{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,10,3]],"date-time":"2026-10-03T23:07:40Z","timestamp":1791068860637,"version":"4.1.0"},"reference-count":232,"publisher":"Elsevier BV","license":[{"start":{"date-parts":[[2021,6,1]],"date-time":"2021-06-01T00:00:00Z","timestamp":1622505600000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/tdm\/userlicense\/1.0\/"},{"start":{"date-parts":[[2021,6,1]],"date-time":"2021-06-01T00:00:00Z","timestamp":1622505600000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/legal\/tdmrep-license"},{"start":{"date-parts":[[2021,6,1]],"date-time":"2021-06-01T00:00:00Z","timestamp":1622505600000},"content-version":"stm-asf","delay-in-days":0,"URL":"https:\/\/doi.org\/10.15223\/policy-017"},{"start":{"date-parts":[[2021,6,1]],"date-time":"2021-06-01T00:00:00Z","timestamp":1622505600000},"content-version":"stm-asf","delay-in-days":0,"URL":"https:\/\/doi.org\/10.15223\/policy-037"},{"start":{"date-parts":[[2021,6,1]],"date-time":"2021-06-01T00:00:00Z","timestamp":1622505600000},"content-version":"stm-asf","delay-in-days":0,"URL":"https:\/\/doi.org\/10.15223\/policy-012"},{"start":{"date-parts":[[2021,6,1]],"date-time":"2021-06-01T00:00:00Z","timestamp":1622505600000},"content-version":"stm-asf","delay-in-days":0,"URL":"https:\/\/doi.org\/10.15223\/policy-029"},{"start":{"date-parts":[[2021,6,1]],"date-time":"2021-06-01T00:00:00Z","timestamp":1622505600000},"content-version":"stm-asf","delay-in-days":0,"URL":"https:\/\/doi.org\/10.15223\/policy-004"}],"content-domain":{"domain":["elsevier.com","sciencedirect.com"],"crossmark-restriction":true},"short-container-title":["Biophysical Chemistry"],"published-print":{"date-parts":[[2021,6]]},"DOI":"10.1016\/j.bpc.2021.106565","type":"journal-article","created":{"date-parts":[[2021,2,25]],"date-time":"2021-02-25T19:14:46Z","timestamp":1614280486000},"page":"106565","update-policy":"https:\/\/doi.org\/10.1016\/elsevier_cm_policy","source":"Crossref","is-referenced-by-count":16,"special_numbering":"C","title":["The structural reconformation of peptides in enhancing functional and therapeutic properties: Insights into their solid state crystallizations"],"prefix":"10.1016","volume":"273","author":[{"given":"Sami","family":"Saadi","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Hasanah Mohd","family":"Ghazali","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Nazamid","family":"Saari","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Sabo Mohammed","family":"Abdulkarim","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"78","reference":[{"key":"10.1016\/j.bpc.2021.106565_bb0005","doi-asserted-by":"crossref","first-page":"419","DOI":"10.1007\/s13594-012-0066-5","article-title":"A mini-review on health and nutritional aspects of cheese with a focus on bioactive peptides","volume":"92","author":"L\u00f3pez-Exp\u00f3sito","year":"2012","journal-title":"Dairy Sci. Technol."},{"issue":"8","key":"10.1016\/j.bpc.2021.106565_bb0010","doi-asserted-by":"crossref","first-page":"953","DOI":"10.3109\/09637486.2013.821696","article-title":"Antioxidant capacity of water soluble extractsfrom Parmigiano-Reggiano cheese","volume":"64","author":"Bottesini","year":"2013","journal-title":"Int. J. Food Sci. Nutr."},{"key":"10.1016\/j.bpc.2021.106565_bb0015","doi-asserted-by":"crossref","first-page":"5447","DOI":"10.1021\/pr4003273","article-title":"Analysis of the endogenous peptide profile of milk: Identification of 248 mainly casein derivedpeptides","volume":"12","author":"Baum","year":"2013","journal-title":"J. Proteome Res."},{"issue":"1","key":"10.1016\/j.bpc.2021.106565_bb0020","doi-asserted-by":"crossref","first-page":"3","DOI":"10.15567\/mljekarstvo.2017.0101","article-title":"White cheeses as a potential source of bioactive peptides","volume":"67","author":"Bara\u0107","year":"2017","journal-title":"Mljekarstvo."},{"key":"10.1016\/j.bpc.2021.106565_bb0025","doi-asserted-by":"crossref","first-page":"26","DOI":"10.1016\/j.idairyj.2014.10.007","article-title":"Differences in the peptide profile of raw and pasteurised ovine milk cheese and implications for its bioactive potential","volume":"42","author":"Pisanu","year":"2015","journal-title":"Int. Dairy J."},{"issue":"1","key":"10.1016\/j.bpc.2021.106565_bb0030","doi-asserted-by":"crossref","first-page":"18","DOI":"10.1039\/C0FO00016G","article-title":"Bioactive peptides derived from milk proteins and their health beneficial potentials: an update","volume":"2","author":"Nagpal","year":"2011","journal-title":"Food Funct."},{"issue":"3-4","key":"10.1016\/j.bpc.2021.106565_bb0035","doi-asserted-by":"crossref","first-page":"153","DOI":"10.1039\/c1fo10017c","article-title":"The potential role of milk-derived peptides in cardiovascular disease","volume":"2","author":"Phelan","year":"2011","journal-title":"Food Funct."},{"issue":"2","key":"10.1016\/j.bpc.2021.106565_bb0040","doi-asserted-by":"crossref","first-page":"177","DOI":"10.1016\/j.jff.2009.01.007","article-title":"Milk derived bioactive peptides: from science to application","volume":"1","author":"Korhonen","year":"2009","journal-title":"J. Funct. Foods"},{"issue":"1","key":"10.1016\/j.bpc.2021.106565_bb0045","doi-asserted-by":"crossref","first-page":"5","DOI":"10.17306\/J.AFS.2014.1.1","article-title":"Milk proteins-derived bioactive peptides in dairy products: molecular, biological and methodological aspects","volume":"13","author":"Dziuba","year":"2014","journal-title":"Acta Sci. Pol. Technol. Aliment."},{"key":"10.1016\/j.bpc.2021.106565_bb0050","doi-asserted-by":"crossref","first-page":"190","DOI":"10.1002\/(SICI)1521-3803(19990601)43:3<190::AID-FOOD190>3.0.CO;2-A","article-title":"Database of biologically active peptide sequences","volume":"43","author":"Dziuba","year":"1999","journal-title":"Nahrung."},{"key":"10.1016\/j.bpc.2021.106565_bb0055","series-title":"Enzymatic modification of food components","first-page":"219","article-title":"Research strategy for proteins and bioactive peptides","author":"Dziuba","year":"2005"},{"key":"10.1016\/j.bpc.2021.106565_bb0060","doi-asserted-by":"crossref","first-page":"82","DOI":"10.1016\/j.idairyj.2012.10.015","article-title":"The comparative assessment of ACE-inhibitory and antioxidant activities of peptide fractions obtained from fermented camel and bovine milk by LactobacillusrhamnosusPTCC 1637","volume":"29","author":"Moslehishad","year":"2013","journal-title":"Int. Dairy J."},{"key":"10.1016\/j.bpc.2021.106565_bb0065","doi-asserted-by":"crossref","first-page":"439","DOI":"10.1007\/s00299-011-1215-7","article-title":"The use of plants for the production of therapeutic human peptides","volume":"31","author":"Lico","year":"2012","journal-title":"Plant Cell Rep."},{"key":"10.1016\/j.bpc.2021.106565_bb0070","doi-asserted-by":"crossref","first-page":"40","DOI":"10.1016\/j.drudis.2009.10.009","article-title":"Synthetic therapeutic peptides: science and market","volume":"15","author":"Vlieghe","year":"2010","journal-title":"Drug Discov. Today"},{"key":"10.1016\/j.bpc.2021.106565_bb0075","doi-asserted-by":"crossref","first-page":"122","DOI":"10.2174\/138920109787048634","article-title":"Advances in peptide pharmaceuticals","volume":"10","author":"Stevenson","year":"2009","journal-title":"Curr. Pharm. Biotechnol."},{"issue":"1","key":"10.1016\/j.bpc.2021.106565_bb0080","first-page":"141","article-title":"Effect of enzymatic hydrolysis on Angiotensin converting enzyme (ACE) inhibitory activity in swiftlet saliva","volume":"23","author":"Nurfatin","year":"2016","journal-title":"Int. Food Res. J."},{"key":"10.1016\/j.bpc.2021.106565_bb0085","doi-asserted-by":"crossref","first-page":"140","DOI":"10.1016\/j.antiviral.2006.02.005","article-title":"Edible bird\u2019s nest extract inhibits influenza virus infection","volume":"70","author":"Guo","year":"2006","journal-title":"Antivir. Res."},{"key":"10.1016\/j.bpc.2021.106565_bb0090","first-page":"521","article-title":"Potentiation of mitogenic response by extracts of the swiftlet\u2019s (Collocalia) nest","volume":"13","author":"Ng","year":"1986","journal-title":"Biochem. Int."},{"key":"10.1016\/j.bpc.2021.106565_bb0095","first-page":"221","article-title":"Evidence that epidermal growth factor is present in swiftlet\u2019s (Collocalia) nest","volume":"87","author":"Kong","year":"1987","journal-title":"Comp. Biochem. Physiol."},{"key":"10.1016\/j.bpc.2021.106565_bb0100","doi-asserted-by":"crossref","first-page":"247","DOI":"10.1111\/1541-4337.12250","article-title":"Sheep milk: physicochemical characteristics and relevance for functional food development","volume":"16","author":"Balthazar","year":"2017","journal-title":"Comp. Rev. Food Sci. Food Safety."},{"key":"10.1016\/j.bpc.2021.106565_bb0105","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1016\/j.smallrumres.2008.12.016","article-title":"Are camel milk proteins convenient to the nutrition of cow milk allergic children?","volume":"82","author":"El-Agamy","year":"2009","journal-title":"Small Rumin. Res."},{"key":"10.1016\/j.bpc.2021.106565_bb0110","doi-asserted-by":"crossref","first-page":"57","DOI":"10.1016\/j.smallrumres.2008.07.009","article-title":"Composition of goat and sheep milk products: an update","volume":"79","author":"Raynal-Ljutovac","year":"2008","journal-title":"Small Rumin. Res."},{"key":"10.1016\/j.bpc.2021.106565_bb0115","doi-asserted-by":"crossref","first-page":"389","DOI":"10.1016\/j.ifset.2014.02.012","article-title":"Functional Pecorino cheese production by using innovative lamb rennet paste","volume":"26","author":"Santillo","year":"2014","journal-title":"Innovative Food Sci. Emerg. Technol."},{"issue":"1","key":"10.1016\/j.bpc.2021.106565_bb0120","doi-asserted-by":"crossref","first-page":"80","DOI":"10.1016\/j.biotechadv.2014.12.003","article-title":"Recent advances in food biopeptides: Production, biological functionalities and therapeutic applications","volume":"33","author":"Saadi","year":"2015","journal-title":"Biotechnol. Adv."},{"key":"10.1016\/j.bpc.2021.106565_bb0125","doi-asserted-by":"crossref","first-page":"93","DOI":"10.1016\/j.jconrel.2017.10.011","article-title":"Smart electrical bi-layers lipopeptides: Novel peptidic chains like zigzag map esterified with phospho-glyceride as mono-layer moieties capable in forming a meso-sphere- envelop with scaffold ability to cellular impurities*","volume":"274","author":"Saadi","year":"2018","journal-title":"Control Release"},{"key":"10.1016\/j.bpc.2021.106565_bb0130","doi-asserted-by":"crossref","first-page":"626","DOI":"10.1093\/ajcn\/80.3.626","article-title":"Fish intake is associated with a reduced progression of coronary artery atherosclerosis in postmenopausal women with coronary heart disease","volume":"80","author":"Erkkila","year":"2004","journal-title":"Am. J. Clin. Nutr."},{"issue":"3","key":"10.1016\/j.bpc.2021.106565_bb0135","first-page":"31","article-title":"Marine fish derived bioactive peptides and proteins and proteins for human therapeutics","volume":"5","author":"Khora","year":"2013","journal-title":"Int J Pharm Pharm Sci"},{"key":"10.1016\/j.bpc.2021.106565_bb0140","doi-asserted-by":"crossref","first-page":"710","DOI":"10.1161\/01.HYP.32.4.710","article-title":"Effects of dietary fish and weight reduction on ambulatory blood pressure in overweight hypertensives","volume":"32","author":"Bao","year":"1998","journal-title":"Hypertension."},{"key":"10.1016\/j.bpc.2021.106565_bb0145","doi-asserted-by":"crossref","first-page":"301","DOI":"10.1042\/bj2380301","article-title":"Properties of signal-sequence peptides at an air-water interface","volume":"238","author":"Fidelio","year":"1986","journal-title":"Biochem. J."},{"key":"10.1016\/j.bpc.2021.106565_bb0150","doi-asserted-by":"crossref","first-page":"314","DOI":"10.1126\/science.177.4046.314","article-title":"Bee and wasp venoms","volume":"177","author":"Habermann","year":"1972","journal-title":"Science."},{"key":"10.1016\/j.bpc.2021.106565_bb0155","doi-asserted-by":"crossref","first-page":"105","DOI":"10.1016\/0022-2836(82)90515-0","article-title":"A simple method for displaying the hydropathic character of a protein","volume":"157","author":"Kyte","year":"1982","journal-title":"J. Mol. Biol."},{"key":"10.1016\/j.bpc.2021.106565_bb0160","doi-asserted-by":"crossref","first-page":"565","DOI":"10.1111\/j.1432-1033.1982.tb07002.x","article-title":"Structural prediction of membrane-bound proteins","volume":"128","author":"Argos","year":"1982","journal-title":"Eur. J. Biochem."},{"key":"10.1016\/j.bpc.2021.106565_bb0165","doi-asserted-by":"crossref","first-page":"3021","DOI":"10.1002\/j.1460-2075.1986.tb04601.x","article-title":"The distribution of positively charged residues in bacterial inner membrane proteins correlates with the trans-membrane topology","volume":"5","author":"von Heijne","year":"1986","journal-title":"EMBO J."},{"key":"10.1016\/j.bpc.2021.106565_bb0170","doi-asserted-by":"crossref","first-page":"1027","DOI":"10.1016\/j.jmb.2004.03.016","article-title":"A combined transmembrane topology and signal peptide prediction method","volume":"338","author":"K\u00e4ll","year":"2004","journal-title":"J. Mol. Biol."},{"key":"10.1016\/j.bpc.2021.106565_bb0175","doi-asserted-by":"crossref","first-page":"4683","DOI":"10.1093\/nar\/14.11.4683","article-title":"A new method for predicting signal sequence cleavage sites","volume":"14","author":"von Heijne","year":"1986","journal-title":"Nucleic Acids Res."},{"key":"10.1016\/j.bpc.2021.106565_bb0180","doi-asserted-by":"crossref","first-page":"257","DOI":"10.1109\/5.18626","article-title":"A tutorial on hidden Markov models and selected applications in speech recognition","volume":"77","author":"Rabiner","year":"1989","journal-title":"Proc. IEEE"},{"key":"10.1016\/j.bpc.2021.106565_bb0185","doi-asserted-by":"crossref","first-page":"136","DOI":"10.1002\/1097-0134(20010101)42:1<136::AID-PROT130>3.0.CO;2-F","article-title":"Prediction of protein signal sequences and their cleavage sites","volume":"42","author":"Chou","year":"2001","journal-title":"Proteins Struct. Funct. Genet."},{"key":"10.1016\/j.bpc.2021.106565_bb0190","first-page":"649","article-title":"Support vector machine prediction of signal peptide cleavage site using a new class of kernels for strings","author":"Vert","year":"2002","journal-title":"Pac. Symp. Biocomput."},{"issue":"2","key":"10.1016\/j.bpc.2021.106565_bb0195","doi-asserted-by":"crossref","first-page":"62","DOI":"10.1016\/j.tifs.2011.08.010","article-title":"Rethinking food-derived bioactive peptides for antimicrobial and immunomodulatory activities","volume":"23","author":"Agyei","year":"2012","journal-title":"Trends Food Sci. Technol."},{"issue":"2","key":"10.1016\/j.bpc.2021.106565_bb0200","doi-asserted-by":"crossref","first-page":"213","DOI":"10.1016\/j.cis.2010.06.010","article-title":"Structured emulsion-based delivery systems: controlling the digestion and release of lipophilic food components","volume":"159","author":"McClements","year":"2010","journal-title":"Adv. Colloid Interf. Sci."},{"issue":"1","key":"10.1016\/j.bpc.2021.106565_bb0205","doi-asserted-by":"crossref","first-page":"R30","DOI":"10.1111\/j.1750-3841.2009.01452.x","article-title":"Design of nano-laminated coatings to control bioavailability of lipophilic food components","volume":"75","author":"McClements","year":"2010","journal-title":"J. Food Sci."},{"key":"10.1016\/j.bpc.2021.106565_bb0210","doi-asserted-by":"crossref","first-page":"48","DOI":"10.7455\/ijfs\/2.1.2013.a4","article-title":"Viability of the microencapsulation of a casein hydrolysate in lipid microparticles of cupuacu butter and stearic acid","volume":"2","author":"Silva","year":"2013","journal-title":"Int. J. Food Stud."},{"key":"10.1016\/j.bpc.2021.106565_bb0215","series-title":"Handbook of Chemistry and Physics 72nd edition","author":"Lide","year":"1991"},{"key":"10.1016\/j.bpc.2021.106565_bb0220","doi-asserted-by":"crossref","first-page":"34682","DOI":"10.1074\/jbc.M402999200","article-title":"Cell-permeable peptide antioxidants targeted to inner mitochondrial membrane inhibit mitochondrial swelling, oxidative cell death, and reperfusion injury","volume":"279","author":"Zhao","year":"2004","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.bpc.2021.106565_bb0225","doi-asserted-by":"crossref","first-page":"4575","DOI":"10.2174\/09298673113209990147","article-title":"Antioxidative peptides: trends and perspectives for future research","volume":"20","author":"Freitas","year":"2013","journal-title":"Curr. Med. Chem."},{"key":"10.1016\/j.bpc.2021.106565_bb0230","doi-asserted-by":"crossref","first-page":"1666","DOI":"10.1021\/cb300281t","article-title":"Isolation and functional characterization of peptide agonists of PTPRJ, a tyrosine phosphatase receptor endowed with tumor suppressor activity","volume":"7","author":"Paduano","year":"2012","journal-title":"ACS Chem. Biol."},{"key":"10.1016\/j.bpc.2021.106565_bb0235","doi-asserted-by":"crossref","first-page":"657","DOI":"10.1016\/j.foodres.2012.06.006","article-title":"The impact of single and double hydrogen bonds on crystallization and melting regimes of Ajwa and Barni lipids","volume":"48","author":"Galeb","year":"2012","journal-title":"Food Res. Int."},{"key":"10.1016\/j.bpc.2021.106565_bb0240","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1088\/0957-4484\/27\/40\/402002","article-title":"Self-assembled peptide nanostructures for functional materials","volume":"27","author":"Ekiz","year":"2016","journal-title":"Nanotechnology."},{"key":"10.1016\/j.bpc.2021.106565_bb0245","doi-asserted-by":"crossref","first-page":"1509","DOI":"10.1002\/1521-3773(20020503)41:9<1509::AID-ANIE1509>3.0.CO;2-K","article-title":"Protein-inspired materials: synthetic concepts and potential applications","volume":"41","author":"Klok","year":"2002","journal-title":"Angew. Chem. Int. Ed."},{"key":"10.1016\/j.bpc.2021.106565_bb0250","doi-asserted-by":"crossref","first-page":"241","DOI":"10.1039\/B906701A","article-title":"Amphiphilic peptides and their cross-disciplinary role as building blocks for nanoscience","volume":"39","author":"Cavalli","year":"2010","journal-title":"Chem. Soc. Rev."},{"key":"10.1016\/j.bpc.2021.106565_bb0255","doi-asserted-by":"crossref","first-page":"1826","DOI":"10.1039\/C1CS15214A","article-title":"Microwave heating in solid-phase peptide synthesis","volume":"41","author":"Pedersen","year":"2012","journal-title":"Chem. Soc. Rev."},{"key":"10.1016\/j.bpc.2021.106565_bb0260","doi-asserted-by":"crossref","first-page":"513","DOI":"10.1152\/physrev.00013.2014","article-title":"Physiology of proglucagon peptides: Role of glucagon and GLP-1 in health and disease","volume":"95","author":"Sandoval","year":"2015","journal-title":"Physiol. Rev."},{"key":"10.1016\/j.bpc.2021.106565_bb0265","doi-asserted-by":"crossref","first-page":"926","DOI":"10.1007\/s00125-004-1380-0","article-title":"Protein hydrolysates stimulate proglucagon gene transcription in intestinal endocrine cells via two elements related to cyclic AMP response element","volume":"47","author":"Gevrey","year":"2004","journal-title":"Diabetologia."},{"key":"10.1016\/j.bpc.2021.106565_bb0270","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1016\/j.cellsig.2009.09.032","article-title":"New insights into the role of cAMP in the production and function of theincretin hormone glucagon-like peptide-1 (GLP-1)","volume":"22","author":"Yu","year":"2010","journal-title":"Cell. Signal."},{"key":"10.1016\/j.bpc.2021.106565_bb0275","doi-asserted-by":"crossref","first-page":"4664","DOI":"10.1210\/en.2006-0274","article-title":"Antidiabetic activity of a highly potent and selective nonpeptidesomatostatin receptor subtype-2 agonist","volume":"147","author":"Strowski","year":"2006","journal-title":"Endocrinology."},{"key":"10.1016\/j.bpc.2021.106565_bb0280","doi-asserted-by":"crossref","first-page":"1700","DOI":"10.1007\/s00125-005-1878-0","article-title":"Alpha cell function in health and disease: influence of glucagon-like peptide-1","volume":"48","author":"Dunning","year":"2005","journal-title":"Diabetologia."},{"key":"10.1016\/j.bpc.2021.106565_bb0285","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1146\/annurev.nutr.26.061505.111258","article-title":"Fuel metabolism in starvation","volume":"26","author":"Cahill","year":"2006","journal-title":"Annu. Rev. Nutr."},{"key":"10.1016\/j.bpc.2021.106565_bb0290","doi-asserted-by":"crossref","first-page":"3727","DOI":"10.1182\/blood-2005-06-2259","article-title":"TLR4-dependent hepcidin expression by myeloid cells in response to bacterial pathogens","volume":"107","author":"Peyssonnaux","year":"2006","journal-title":"Blood."},{"key":"10.1016\/j.bpc.2021.106565_bb0295","doi-asserted-by":"crossref","first-page":"2663","DOI":"10.1210\/en.2006-1331","article-title":"The iron regulatory peptide hepcidin is expressed in the heart and regulated by hypoxia and inflammation","volume":"148","author":"Merle","year":"2007","journal-title":"Endocrinology."},{"key":"10.1016\/j.bpc.2021.106565_bb0300","doi-asserted-by":"crossref","first-page":"361","DOI":"10.1677\/joe.1.05729","article-title":"The iron-regulatory peptide hormone hepcidin: expression and cellular localization in the mammalian kidney","volume":"184","author":"Kulaksiz","year":"2005","journal-title":"J. Endocrinol."},{"key":"10.1016\/j.bpc.2021.106565_bb0305","doi-asserted-by":"crossref","first-page":"241","DOI":"10.1677\/JOE-07-0528","article-title":"Pancreatic beta-cells express hepcidin, an iron-uptake regulatory peptide","volume":"197","author":"Kulaksiz","year":"2008","journal-title":"J. Endocrinol."},{"key":"10.1016\/j.bpc.2021.106565_bb0310","doi-asserted-by":"crossref","first-page":"749","DOI":"10.1016\/j.jnutbio.2009.04.009","article-title":"Expression of the peptide hormone hepcidin increases in cardiomyocytesunder myocarditis and myocardial infarction","volume":"21","author":"Isoda","year":"2010","journal-title":"J. Nutr. Biochem."},{"key":"10.1016\/j.bpc.2021.106565_bb0315","doi-asserted-by":"crossref","first-page":"883","DOI":"10.1111\/j.1365-2362.2009.02182.x","article-title":"Serum hepcidin concentration in chronic haemodialysis patients: associations and effects of dialysis, iron and erythropoietin therapy","volume":"39","author":"Weiss","year":"2009","journal-title":"Eur. J. Clin. Investig."},{"key":"10.1016\/j.bpc.2021.106565_bb0320","doi-asserted-by":"crossref","first-page":"943","DOI":"10.1093\/eurjhf\/hfq099","article-title":"Hepcidin-25 is a marker of the response rather than resistance to exogenous erythropoietin in chronic kidney disease\/chronic heart failure patients","volume":"12","author":"van der Putten","year":"2010","journal-title":"Eur. J. Heart Fail."},{"key":"10.1016\/j.bpc.2021.106565_bb0325","doi-asserted-by":"crossref","first-page":"1485","DOI":"10.1016\/j.foodchem.2012.02.038","article-title":"Crystallisation regime of w\/o emulsion [e.g. multipurpose margarine] models during storage","volume":"133","author":"Saadi","year":"2012","journal-title":"Food Chem."},{"key":"10.1016\/j.bpc.2021.106565_bb0330","doi-asserted-by":"crossref","first-page":"453","DOI":"10.1016\/j.metabol.2004.10.012","article-title":"Iron loading increases cholesterol accumulation and macrophage scavenger receptor I expression in THP-1 mononuclear phagocytes","volume":"54","author":"Kraml","year":"2005","journal-title":"Metabolism."},{"key":"10.1016\/j.bpc.2021.106565_bb0335","doi-asserted-by":"crossref","first-page":"1014","DOI":"10.3181\/0703-MR-54","article-title":"Macrophage iron, hepcidin, and atherosclerotic plaque stability","volume":"232","author":"Sullivan","year":"2007","journal-title":"Exp. Biol. Med."},{"key":"10.1016\/j.bpc.2021.106565_bb0340","doi-asserted-by":"crossref","first-page":"660","DOI":"10.1016\/S0955-2863(97)00113-7","article-title":"Nutritional biochemistry of cellular glutathione","volume":"8","author":"Sen","year":"1997","journal-title":"Nutr. Biochem."},{"key":"10.1016\/j.bpc.2021.106565_bb0345","doi-asserted-by":"crossref","first-page":"191","DOI":"10.1515\/BC.2009.033","article-title":"Glutathione dysregulation and the etiology and progression of human diseases","volume":"390","author":"Ballatori","year":"2009","journal-title":"Biol. Chem."},{"key":"10.1016\/j.bpc.2021.106565_bb0350","doi-asserted-by":"crossref","DOI":"10.1016\/j.peptides.2012.09.011","article-title":"Antioxidant activity of vasoactive intestinal peptide in HK2 human renal cells","author":"Vacas","year":"2012","journal-title":"Peptides"},{"key":"10.1016\/j.bpc.2021.106565_bb0355","doi-asserted-by":"crossref","first-page":"51","DOI":"10.1007\/s12031-011-9618-z","article-title":"Antioxidant and anti-apoptotic activity of vasoactive intestinal peptide (VIP) against 6-hydroxy dopamine toxicity in the rat corpus striatum","volume":"46","author":"Tun\u00e7el","year":"2012","journal-title":"J. Mol. Neurosci."},{"key":"10.1016\/j.bpc.2021.106565_bb0360","doi-asserted-by":"crossref","first-page":"1872","DOI":"10.1016\/j.foodchem.2011.12.020","article-title":"An active peptide purified grom gastrointestinal enzyme hydrolysate of Pacific cod skin gelatin attenuates angiotensin-1 converting enzyme (ACE) activityand cellular oxidative stress","volume":"132","author":"Himaya","year":"2012","journal-title":"Food Chem."},{"issue":"4","key":"10.1016\/j.bpc.2021.106565_bb0365","first-page":"447","article-title":"Determination of hippuric acid by RPHPLC using two different analytical columns-A short report","volume":"57","author":"Pegg","year":"2007","journal-title":"Polish J. Food Nutr. Sci."},{"key":"10.1016\/j.bpc.2021.106565_bb0370","doi-asserted-by":"crossref","first-page":"6981","DOI":"10.1021\/jf025592e","article-title":"Peptides with angiotensin I-converting enzyme inhibitory activity from defibrinated hydrolyzed bovine plasma","volume":"50","author":"Wanasundara","year":"2002","journal-title":"J. Agric. Food Chem."},{"key":"10.1016\/j.bpc.2021.106565_bb0375","doi-asserted-by":"crossref","first-page":"4637","DOI":"10.1073\/pnas.94.9.4637","article-title":"Direct antidiabetic effect of leptin through triglyceride depletion of tissues","volume":"94","author":"Shimabukuro","year":"1997","journal-title":"Proc. Natl. Acad. Sci. U. S. A."},{"key":"10.1016\/j.bpc.2021.106565_bb0380","doi-asserted-by":"crossref","first-page":"614","DOI":"10.1016\/0042-6822(88)90302-9","article-title":"A simple technique for the rescue of the early region 1 into infectious human adenovirus type 5","volume":"163","author":"McCrory","year":"1988","journal-title":"Virology."},{"key":"10.1016\/j.bpc.2021.106565_bb0385","doi-asserted-by":"crossref","first-page":"14795","DOI":"10.1073\/pnas.93.25.14795","article-title":"Disappearance of body fat in normal rats induced by adenovirus\u2013mediated leptin genes therapy","volume":"93","author":"Chen","year":"1996","journal-title":"Proc. Natl. Acad. Sci. U. S. A."},{"key":"10.1016\/j.bpc.2021.106565_bb0390","doi-asserted-by":"crossref","first-page":"13939","DOI":"10.1074\/jbc.271.24.13939","article-title":"Obese gene expression alters the ability of 30A5 preadipocytesto repond to lipogenic hormones","volume":"271","author":"Bai","year":"1996","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.bpc.2021.106565_bb0395","doi-asserted-by":"crossref","first-page":"4382","DOI":"10.1016\/S0021-9258(19)63806-8","article-title":"Ketone body metabolism in the ketosis of starvation and alloxan diabetes","volume":"245","author":"McGarry","year":"1970","journal-title":"J. Biol. Chem."},{"issue":"15","key":"10.1016\/j.bpc.2021.106565_bb0400","doi-asserted-by":"crossref","first-page":"1201","DOI":"10.1016\/j.jacc.2008.05.060","article-title":"Leptin Resistance: a possible interface of inflammation and metabolism in obesity-related cardiovascular disease","volume":"52","author":"Martin","year":"2008","journal-title":"J. Am. Coll. Cardiol."},{"key":"10.1016\/j.bpc.2021.106565_bb0405","doi-asserted-by":"crossref","first-page":"820","DOI":"10.1016\/j.biocel.2005.09.013","article-title":"Rethinking leptin and insulin action: therapeutic opportunities for diabetes","volume":"38","author":"Yildiz","year":"2006","journal-title":"Int. J. Biochem. Cell Biol."},{"key":"10.1016\/j.bpc.2021.106565_bb0410","doi-asserted-by":"crossref","first-page":"5629","DOI":"10.1074\/jbc.M008553200","article-title":"Liporegulation in diet-induced obesity. The antisteatotic role of hyperleptinemia","volume":"276","author":"Lee","year":"2001","journal-title":"J. Biol. Chem."},{"issue":"6","key":"10.1016\/j.bpc.2021.106565_bb0415","doi-asserted-by":"crossref","first-page":"942","DOI":"10.1093\/clinchem\/42.6.942","article-title":"Radioimmunoassay of leptin in human plasma","volume":"42","author":"Ma","year":"1996","journal-title":"Clin. Chem."},{"key":"10.1016\/j.bpc.2021.106565_bb0420","doi-asserted-by":"crossref","first-page":"543","DOI":"10.1126\/science.7624777","article-title":"Weight-reducing effects of the plasma protein encoded by the obese gene","volume":"269","author":"Halaas","year":"1995","journal-title":"Science."},{"key":"10.1016\/j.bpc.2021.106565_bb0425","doi-asserted-by":"crossref","first-page":"546","DOI":"10.1126\/science.7624778","article-title":"Recombinant mouse OB protein: evidence for a peripheral signal linking adiposity and central neural networks","volume":"269","author":"Campfield","year":"1995","journal-title":"Science."},{"key":"10.1016\/j.bpc.2021.106565_bb0430","doi-asserted-by":"crossref","first-page":"540","DOI":"10.1126\/science.7624776","article-title":"Effects of the obese gene product on body weight regulation in ob\/obmice","volume":"269","author":"Pelleymounter","year":"1995","journal-title":"Science."},{"key":"10.1016\/j.bpc.2021.106565_bb0435","doi-asserted-by":"crossref","first-page":"950","DOI":"10.1038\/nm0995-950","article-title":"Overexpression of the obese (ob) gene in adipose tissue of human obese subjects","volume":"1","author":"Lonnqvist","year":"1995","journal-title":"Nat. Med."},{"key":"10.1016\/j.bpc.2021.106565_bb0440","doi-asserted-by":"crossref","first-page":"2986","DOI":"10.1172\/JCI118007","article-title":"Evidence against either a premature stop codon or the absence of obese gene mRNA in human obesity","volume":"95","author":"Considine","year":"1995","journal-title":"J. Clin. Invest."},{"key":"10.1016\/j.bpc.2021.106565_bb0445","doi-asserted-by":"crossref","first-page":"953","DOI":"10.1038\/nm0995-953","article-title":"Increased obese mRNA in omental fat cells from massively obese humans","volume":"1","author":"Hamilton","year":"1995","journal-title":"Nat. Med."},{"key":"10.1016\/j.bpc.2021.106565_bb0450","doi-asserted-by":"crossref","first-page":"1155","DOI":"10.1038\/nm1195-1155","article-title":"Leptin levels in human and rodent-measurement of plasma leptin and ob RNA in obese and weight-reduced subjects","volume":"1","author":"Maffei","year":"1995","journal-title":"Nat. Med."},{"key":"10.1016\/j.bpc.2021.106565_bb0455","doi-asserted-by":"crossref","first-page":"1263","DOI":"10.1016\/0092-8674(95)90151-5","article-title":"Identification and expression cloning of a leptin receptor, ob-r","volume":"83","author":"Tartaglia","year":"1995","journal-title":"Cell."},{"key":"10.1016\/j.bpc.2021.106565_bb0460","doi-asserted-by":"crossref","first-page":"446","DOI":"10.1111\/1541-4337.12136","article-title":"Marine bioactive compounds and their health benefits: A review","volume":"14","author":"Hamed","year":"2015","journal-title":"Compr. Rev. Food Sci. Food Saf."},{"key":"10.1016\/j.bpc.2021.106565_bb0465","doi-asserted-by":"crossref","first-page":"1359","DOI":"10.3390\/md9081359","article-title":"Fucoidan from marine brown algae inhibits lipid accumulation","volume":"9","author":"Park","year":"2011","journal-title":"Mar. Drugs"},{"issue":"13","key":"10.1016\/j.bpc.2021.106565_bb0470","doi-asserted-by":"crossref","first-page":"1002","DOI":"10.1016\/j.jacc.2010.03.083","article-title":"Iron overload cardiomyopathy better understanding of an increasing disorder","volume":"56","author":"Gujja","year":"2010","journal-title":"J. Am. Coll. Cardiol."},{"key":"10.1016\/j.bpc.2021.106565_bb0475","doi-asserted-by":"crossref","first-page":"1527","DOI":"10.1126\/science.274.5292.1527","article-title":"Association of anxiety-related traits with a polymorphism in the serotonin transporter gene regulatory region","volume":"274","author":"Murphy","year":"1996","journal-title":"Science."},{"key":"10.1016\/j.bpc.2021.106565_bb0480","doi-asserted-by":"crossref","first-page":"4033","DOI":"10.1002\/rcm.3319","article-title":"Simple and sensitive quantification of bioactive peptides in biological matrices using liquid chromatography\/selected reaction monitoring mass spectrometry coupled with trichloroacetic acid clean-up","volume":"21","author":"Murao","year":"2007","journal-title":"Rapid Commun. Mass Spectrom."},{"key":"10.1016\/j.bpc.2021.106565_bb0485","doi-asserted-by":"crossref","first-page":"788","DOI":"10.1053\/j.gastro.2006.07.007","article-title":"Increased adipose tissue expression of hepcidin in severe obesity is independent from diabetes and NASH","volume":"131","author":"Bekri","year":"2006","journal-title":"Gastroenterology."},{"key":"10.1016\/j.bpc.2021.106565_bb0490","doi-asserted-by":"crossref","first-page":"711","DOI":"10.1074\/jbc.R800017200","article-title":"Iron homeostasis: recently identified proteins provide insight into novel control mechanisms","volume":"284","author":"Zhang","year":"2009","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.bpc.2021.106565_bb0495","doi-asserted-by":"crossref","first-page":"425","DOI":"10.1038\/372425a0","article-title":"Positional cloning of the mouse obese gene and its human homologue","volume":"372","author":"Zhang","year":"1994","journal-title":"Nature (London)"},{"key":"10.1016\/j.bpc.2021.106565_bb0500","article-title":"Review of medical physiology, 18th edition","volume":"223","author":"Ganong","year":"1997","journal-title":"Appleton and Lange: New York"},{"key":"10.1016\/j.bpc.2021.106565_bb0505","doi-asserted-by":"crossref","first-page":"1810","DOI":"10.1210\/jcem.83.5.4952","article-title":"Leptin expression in human mammary epithelial cells and breast milk","volume":"83","author":"Smith-Kirwin","year":"1998","journal-title":"J. Clin. Endocrinol. Metab."},{"key":"10.1016\/j.bpc.2021.106565_bb0510","doi-asserted-by":"crossref","first-page":"790","DOI":"10.1038\/29547","article-title":"The stomach is a source of leptin","volume":"394","author":"Bado","year":"1998","journal-title":"Nature (London)"},{"key":"10.1016\/j.bpc.2021.106565_bb0515","first-page":"4459","article-title":"Expression of Ob receptor in normal human adrenals: differential regulation of adrenocortical and adrenomedullary function by leptin","volume":"83","author":"Glasow","year":"1998","journal-title":"J. Clin. Endocrinol. Metab."},{"key":"10.1016\/j.bpc.2021.106565_bb0520","doi-asserted-by":"crossref","first-page":"273","DOI":"10.1016\/S0014-2999(98)00884-X","article-title":"Expression of leptin receptor in lung: leptin as a growth factor","volume":"365","author":"Tsuchiya","year":"1999","journal-title":"Eur. J. Pharmacol."},{"key":"10.1016\/j.bpc.2021.106565_bb0525","doi-asserted-by":"crossref","first-page":"4325","DOI":"10.1158\/1078-0432.CCR-03-0749","article-title":"Enhanced expression of leptin and leptin receptor (OB-R) in human breast cancer","volume":"10","author":"Ishikawa","year":"2004","journal-title":"Clin. Cancer Res."},{"key":"10.1016\/j.bpc.2021.106565_bb0530","doi-asserted-by":"crossref","first-page":"481","DOI":"10.1136\/gut.47.4.481","article-title":"Expression of leptin receptor isoforms in the human stomach","volume":"47","author":"Mix","year":"2000","journal-title":"Gut."},{"key":"10.1016\/j.bpc.2021.106565_bb0535","doi-asserted-by":"crossref","first-page":"424","DOI":"10.1093\/jjco\/hye097","article-title":"Effect of tamoxifen on the serum leptin level in patients with breast cancer","volume":"31","author":"Ozet","year":"2001","journal-title":"Jpn. J. Clin. Oncol."},{"key":"10.1016\/j.bpc.2021.106565_bb0540","doi-asserted-by":"crossref","first-page":"357","DOI":"10.1079\/BJN20041189","article-title":"Bioavailability of angiotensin I converting enzyme inhibitory peptides","volume":"92","author":"Vermeirssen","year":"2004","journal-title":"Br. J. Nutr."},{"key":"10.1016\/j.bpc.2021.106565_bb0545","doi-asserted-by":"crossref","first-page":"785","DOI":"10.1016\/0196-9781(95)00054-N","article-title":"Isolation and characterization of ovokinin, a bradykinin B-1 agonist peptide derived from ovalbumin","volume":"16","author":"Fujita","year":"1995","journal-title":"Peptides."},{"key":"10.1016\/j.bpc.2021.106565_bb0550","doi-asserted-by":"crossref","first-page":"181","DOI":"10.1016\/S0014-5793(99)00587-6","article-title":"A novel antihypertensive peptide derived from ovalbumin induces nitric oxide-mediated vasorelaxation in an isolated SHR mesenteric artery","volume":"452","author":"Matoba","year":"1999","journal-title":"FEBS Lett."},{"issue":"2","key":"10.1016\/j.bpc.2021.106565_bb0555","doi-asserted-by":"crossref","first-page":"401","DOI":"10.1016\/S0021-9258(19)86187-2","article-title":"Binding of peptide substrates and inhibitors of angiotensin-converting enzyme: The importance of COOH terminal dipeptide sequence","volume":"255","author":"Cheung","year":"1980","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.bpc.2021.106565_bb0560","doi-asserted-by":"crossref","first-page":"3845","DOI":"10.1016\/S0021-9258(19)41475-0","article-title":"Insulin and epidermal growth factor. Human fibroblast receptors related to deoxyribonucleic acid synthesis and amino acid uptake","volume":"250","author":"Hollenberg","year":"1975","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.bpc.2021.106565_bb0565","doi-asserted-by":"crossref","first-page":"159","DOI":"10.1083\/jcb.71.1.159","article-title":"125I-labelled human epidermal growth factor. Binding, internalization, and degradation in human fibroblasts","volume":"71","author":"Carpenter","year":"1976","journal-title":"J. Cell Biol."},{"issue":"6","key":"10.1016\/j.bpc.2021.106565_bb0570","doi-asserted-by":"crossref","first-page":"2644","DOI":"10.1073\/pnas.75.6.2644","article-title":"Molecular mechanism of mitogen action: processing of receptor induced by epidermal growth factor","volume":"75","author":"Das","year":"1978","journal-title":"Proc. Natl. Acad. Sci. U. S. A."},{"key":"10.1016\/j.bpc.2021.106565_bb0575","doi-asserted-by":"crossref","first-page":"3","DOI":"10.1159\/000066656","article-title":"The renin-angiotensin system and progression or renal disease: From hemodynamics to cell biology","volume":"93","author":"Wolf","year":"2003","journal-title":"Nephron. Physiol."},{"key":"10.1016\/j.bpc.2021.106565_bb0580","doi-asserted-by":"crossref","first-page":"2346","DOI":"10.1681\/ASN.2004060458","article-title":"N-acetylcysteine decreases angiotensin II receptor binding in vascular smooth muscle cells","volume":"16","author":"Ullian","year":"2005","journal-title":"J. Am. Soc. Nephrol."},{"key":"10.1016\/j.bpc.2021.106565_bb0585","doi-asserted-by":"crossref","first-page":"2985","DOI":"10.1681\/ASN.2006040356","article-title":"Renin-angiotensin-aldosterone system and progression of renal disease","volume":"17","author":"R\u00fcster","year":"2006","journal-title":"J. Am. Soc. Nephrol."},{"key":"10.1016\/j.bpc.2021.106565_bb0590","doi-asserted-by":"crossref","first-page":"148","DOI":"10.1038\/375148a0","article-title":"Serial triggering of many T-cell receptors by a few peptides-MHC complexes","volume":"375","author":"Valitutti","year":"1995","journal-title":"Nature."},{"issue":"7","key":"10.1016\/j.bpc.2021.106565_bb0595","doi-asserted-by":"crossref","first-page":"2735","DOI":"10.1073\/pnas.92.7.2735","article-title":"Gentic control of blood pressure and the angiotensinogen locus","volume":"92","author":"Kim","year":"1995","journal-title":"Proc. Natl. Acad. Sci. U. S. A."},{"key":"10.1016\/j.bpc.2021.106565_bb0600","doi-asserted-by":"crossref","first-page":"509","DOI":"10.1007\/BF00484623","article-title":"Genetic and endocrine control of renin activity in the submaxillary gland of the mouse","volume":"19","author":"Wilson","year":"1981","journal-title":"Biochem. Genet."},{"key":"10.1016\/j.bpc.2021.106565_bb0605","doi-asserted-by":"crossref","first-page":"1761","DOI":"10.1681\/ASN.V5101761","article-title":"Renal hemodynamics and plasma and kidney angiotensin II in established diabetes mellitus in rats: Effect of sodium and salt restriction","volume":"5","author":"Vallon","year":"1995","journal-title":"J. Am. Soc. Nephrol."},{"issue":"1","key":"10.1016\/j.bpc.2021.106565_bb0610","doi-asserted-by":"crossref","first-page":"153","DOI":"10.1016\/S0272-6386(97)90023-8","article-title":"The role of angiotensin II in diabetic nephropathy: emphasis on non-hemodynamic mechanisms","volume":"29","author":"Wolf","year":"1997","journal-title":"Am. J. Kidney Dis."},{"key":"10.1016\/j.bpc.2021.106565_bb0615","series-title":"Angiotensin Converting Enzyme Inhibitors","article-title":"ACE inhibitor for hypertension","author":"Opie","year":"1992"},{"key":"10.1016\/j.bpc.2021.106565_bb0620","series-title":"Advances in Enzymology and Related Areas of Molecular Biology","first-page":"1","article-title":"The design and properties of N-carboxyalkyldipeptide inhibitors of angiotensin converting enzyme","volume":"Vol. 57","author":"Patchett","year":"1985"},{"issue":"1","key":"10.1016\/j.bpc.2021.106565_bb0625","doi-asserted-by":"crossref","first-page":"3","DOI":"10.1002\/(SICI)1098-1128(199601)16:1<3::AID-MED1>3.0.CO;2-6","article-title":"The art and practice of structure based drug design: a molecular modeling perspective","volume":"16","author":"Bohacek","year":"1996","journal-title":"Med. Res. Rev."},{"key":"10.1016\/j.bpc.2021.106565_bb0630","doi-asserted-by":"crossref","first-page":"1234","DOI":"10.1016\/S0735-1097(96)00277-X","article-title":"Marked expression of plasma brain natriuretic peptide is a special feature of hypertrophic obstructive cardiomyopathy","volume":"28","author":"Nishgaki","year":"1996","journal-title":"J. Am. Coll. Cardiol."},{"key":"10.1016\/j.bpc.2021.106565_bb0635","doi-asserted-by":"crossref","first-page":"9","DOI":"10.1161\/01.RES.71.1.9","article-title":"Expression of A-, B-,C- type natriuretic peptide gene in failing and developing human ventricles: correlation with expression of the Ca2+-ATPase gene","volume":"71","author":"Takahashi","year":"1992","journal-title":"Circ. Res."},{"issue":"1","key":"10.1016\/j.bpc.2021.106565_bb0640","doi-asserted-by":"crossref","first-page":"215","DOI":"10.1152\/physrev.1999.79.1.215","article-title":"Molecular mechanism of myocardial remodeling","volume":"79","author":"Swynghedauw","year":"1999","journal-title":"Physiol. Rev."},{"key":"10.1016\/j.bpc.2021.106565_bb0645","doi-asserted-by":"crossref","first-page":"107","DOI":"10.1016\/S0014-5793(97)01179-4","article-title":"Cardiac myocytes and nbroblasts contain functional estrogen receptors","volume":"416","author":"Groh\u00e9","year":"1997","journal-title":"FEBS Lett."},{"issue":"3","key":"10.1016\/j.bpc.2021.106565_bb0650","doi-asserted-by":"crossref","first-page":"646","DOI":"10.1053\/ajkd.2000.16225","article-title":"Preserving renal function in adults with hypertension and diabetes: a consensus approach","volume":"36","author":"Bakris","year":"2000","journal-title":"Am. J. Kidney Dis."},{"issue":"11","key":"10.1016\/j.bpc.2021.106565_bb0655","doi-asserted-by":"crossref","first-page":"3845","DOI":"10.3168\/jds.S0022-0302(04)73524-9","article-title":"In vitro generation and stability of the lactokinin beta-lactoglobulin fragment (142\u2013148)","volume":"87","author":"Walsh","year":"2004","journal-title":"J. Diary Sci."},{"key":"10.1016\/j.bpc.2021.106565_bb0660","doi-asserted-by":"crossref","first-page":"797","DOI":"10.1007\/s00726-012-1393-9","article-title":"Antioxidative peptides: enzymatic production, in vitro and in vivo antioxidant activity and potential applications of milk-derived antioxidative peptides","volume":"44","author":"Power","year":"2013","journal-title":"Amino Acids"},{"key":"10.1016\/j.bpc.2021.106565_bb0665","doi-asserted-by":"crossref","first-page":"1600","DOI":"10.1016\/S0140-6736(95)90115-9","article-title":"Association of angiotensinogen gene T235 variant with increased risk of coronary heart disease","volume":"345","author":"Katsuya","year":"1995","journal-title":"Lancet."},{"key":"10.1016\/j.bpc.2021.106565_bb0670","doi-asserted-by":"crossref","first-page":"1629","DOI":"10.1056\/NEJM199406093302301","article-title":"Linkage of the angiotensinogen gene to essential hypertension","volume":"330","author":"Caulfield","year":"1994","journal-title":"N. Engl. J. Med."},{"key":"10.1016\/j.bpc.2021.106565_bb0675","doi-asserted-by":"crossref","first-page":"607","DOI":"10.1152\/physrev.00011.2009","article-title":"Physiology of Kidney Renin","volume":"90","author":"Castrop","year":"2010","journal-title":"Physiol. Rev."},{"issue":"90","key":"10.1016\/j.bpc.2021.106565_bb0680","doi-asserted-by":"crossref","first-page":"387","DOI":"10.1016\/j.jsbmb.2004.03.004","article-title":"Vitamin D: a negative endocrine regulator of the renin\u2013angiotensin system and blood pressure","volume":"89","author":"Li","year":"2004","journal-title":"J. Steroid Biochem. Mol. Biol."},{"key":"10.1016\/j.bpc.2021.106565_bb0685","doi-asserted-by":"crossref","first-page":"84","DOI":"10.1079\/BJN20051422","article-title":"Antihypertensive effect of casein hydrolysate in a placebocontrolled study in subjects with high normal blood pressure and mild hypertension","volume":"94","author":"Mizuno","year":"2005","journal-title":"Br. J. Nutr."},{"issue":"2","key":"10.1016\/j.bpc.2021.106565_bb0690","doi-asserted-by":"crossref","first-page":"177","DOI":"10.1016\/j.jff.2009.01.007","article-title":"Milk-derived bioactive peptides: From science to applications","volume":"1","author":"Korhonen","year":"2009","journal-title":"J. Funct. Foods"},{"key":"10.1016\/j.bpc.2021.106565_bb0695","first-page":"1415","article-title":"Specific stimulation and inhibition of renal prostaglandin release by angiotensin analogs","volume":"224","author":"Needleman","year":"1973","journal-title":"Am. J. Phys."},{"key":"10.1016\/j.bpc.2021.106565_bb0700","doi-asserted-by":"crossref","first-page":"678","DOI":"10.1016\/S0022-3565(25)29459-9","article-title":"Intrarenal prostaglandin release attenuates the renal vasoconstrictor activity to angiotensin","volume":"184","author":"Aiken","year":"1976","journal-title":"J. Pharmacol. Exp. Ther."},{"key":"10.1016\/j.bpc.2021.106565_bb0705","doi-asserted-by":"crossref","first-page":"1257","DOI":"10.1172\/JCI109788","article-title":"Captopril-induced changes in prostaglandin production: relationship to Vascular responses in normal man","volume":"65","author":"Swartz","year":"1980","journal-title":"Am. Soc. Clin. Invest."},{"key":"10.1016\/j.bpc.2021.106565_bb0710","doi-asserted-by":"crossref","first-page":"63","DOI":"10.1111\/j.1541-4337.2005.tb00075.x","article-title":"A new frontier in soy bioactive peptides that may prevent age-related chronic diseases","volume":"4","author":"Wang","year":"2005","journal-title":"Compr. Rev. Food Sci. F."},{"key":"10.1016\/j.bpc.2021.106565_bb0715","doi-asserted-by":"crossref","first-page":"885","DOI":"10.1016\/S0006-291X(84)80190-4","article-title":"Alzheimer's disease: initial report of the purification and characterisation of a novel cerebo-vascular amyloid protein","volume":"120","author":"Glenner","year":"1984","journal-title":"Biochem. Biophys. Res. Commun."},{"key":"10.1016\/j.bpc.2021.106565_bb0720","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1046\/j.1471-4159.2002.00855.x","article-title":"\u03b2-Amyloid catabolism: roles for neprilysin (NEP) and other metallopeptidases?","volume":"81","author":"Carsonand","year":"2002","journal-title":"J. Neurochem."},{"issue":"45","key":"10.1016\/j.bpc.2021.106565_bb0725","doi-asserted-by":"crossref","first-page":"37644","DOI":"10.1074\/jbc.M508460200","article-title":"Amyloid \u03b2-protein is degraded by cellular angiotensin converting enzyme (ACE) and elevated by an ACE inhibitor","volume":"280","author":"Hemming","year":"2005","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.bpc.2021.106565_bb0730","doi-asserted-by":"crossref","first-page":"14838","DOI":"10.1074\/jbc.M200581200","article-title":"Hydrolysis of biological peptides by human angiotensin-converting enzyme-related carboxypeptidase","volume":"277","author":"Vickers","year":"2002","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.bpc.2021.106565_bb0735","doi-asserted-by":"crossref","first-page":"15377","DOI":"10.1016\/S0021-9258(18)98626-6","article-title":"Structure of the angiotensin I converting enzyme genes: Two alternate promoters correspond to evolutionary step of a duplicated gene","volume":"266","author":"Hubert","year":"1991","journal-title":"J. Biol. Chem."},{"issue":"43","key":"10.1016\/j.bpc.2021.106565_bb0740","doi-asserted-by":"crossref","first-page":"33238","DOI":"10.1074\/jbc.M002615200","article-title":"A human homolog of angiotensin-converting enzyme: cloning and functional expression as a captopril-insensitive carboxylpeptidase","volume":"275","author":"Tipnis","year":"2000","journal-title":"J. Biol. Chem."},{"issue":"8","key":"10.1016\/j.bpc.2021.106565_bb0745","doi-asserted-by":"crossref","first-page":"3656","DOI":"10.1074\/jbc.270.8.3656","article-title":"The hemoregulatory peptides N-acetyl-Ser-Asp-Lys-Pro is a natural and specific substrate of the N-terminal active site of human angiotensin converting enzyme","volume":"270","author":"Rousseau","year":"1995","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.bpc.2021.106565_bb0750","doi-asserted-by":"crossref","first-page":"9002","DOI":"10.1016\/S0021-9258(18)31543-6","article-title":"The two homologous domains of human angiotensin I-converting enzyme are both catalytically active","volume":"266","author":"Wei","year":"1991","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.bpc.2021.106565_bb0755","doi-asserted-by":"crossref","first-page":"1433","DOI":"10.1093\/nar\/20.6.1433-a","article-title":"PCR detection of the insertion\/deletion polymorphism of the human angiotensin converting enzyme gene (DCP1) (dipeptidyl carboxylpeptidase 1)","volume":"20","author":"Rigat","year":"1992","journal-title":"Nucleic Acids Res."},{"key":"10.1016\/j.bpc.2021.106565_bb0760","doi-asserted-by":"crossref","first-page":"120","DOI":"10.1101\/gr.3.2.120","article-title":"Mistyping ACE heterozygotes","volume":"3","author":"Shanmugam","year":"1993","journal-title":"Genome Res."},{"issue":"6","key":"10.1016\/j.bpc.2021.106565_bb0765","doi-asserted-by":"crossref","first-page":"597","DOI":"10.2174\/138161280306221010120623","article-title":"Endothelin converting enzyme inhibitor","volume":"3","author":"Jeng","year":"1997","journal-title":"Curr. Pharm. Des."},{"key":"10.1016\/j.bpc.2021.106565_bb0770","doi-asserted-by":"crossref","first-page":"1631","DOI":"10.2174\/0929867023369402","article-title":"Hydroxamic acids as pharmacological agents","volume":"9","author":"Muri","year":"2002","journal-title":"Curr. Med. Chem."},{"issue":"3\/4","key":"10.1016\/j.bpc.2021.106565_bb0775","doi-asserted-by":"crossref","first-page":"389","DOI":"10.1080\/08827509808914162","article-title":"Kinetic and interfacial phenomena in solvent extraction of metals","volume":"18","author":"Szymanowski","year":"1998","journal-title":"Miner. Proc. Extract. Metall. Rev."},{"issue":"2","key":"10.1016\/j.bpc.2021.106565_bb0780","doi-asserted-by":"crossref","first-page":"334","DOI":"10.1016\/j.foodchem.2010.08.058","article-title":"Contribution of Leu and Hyp residues to antioxidant and ACE-Inhibitory activities of peptides sequence isolated from squid gelatin hydrolysate","volume":"125","author":"Alem\u00e1n","year":"2011","journal-title":"Food Chem."},{"key":"10.1016\/j.bpc.2021.106565_bb0785","doi-asserted-by":"crossref","first-page":"471","DOI":"10.1136\/bmj.293.6545.471","article-title":"Beneficial effects of angiotensin converting enzyme inhibition on renal function in patients with diabetic nephropathy","volume":"293","author":"Bj\u00f6rck","year":"1986","journal-title":"Br. Med. J."},{"key":"10.1016\/j.bpc.2021.106565_bb0790","doi-asserted-by":"crossref","first-page":"1637","DOI":"10.1016\/0006-2952(71)90292-9","article-title":"Spectrophotometric assay and properties of the angiotensin converting enzyme of rabbit lung","volume":"20","author":"Cushman","year":"1971","journal-title":"Biochem. Pharmacol."},{"key":"10.1016\/j.bpc.2021.106565_bb0795","doi-asserted-by":"crossref","first-page":"501","DOI":"10.1042\/bj1670501","article-title":"A simple radioassay for angiotensin-converting enzyme","volume":"161","author":"Ryan","year":"1977","journal-title":"Biochem. J."},{"key":"10.1016\/j.bpc.2021.106565_bb0800","doi-asserted-by":"crossref","DOI":"10.1172\/JCI110663","article-title":"Induction by glucocorticoids of angiotensin converting enzyme production from bovine endothelial cells in culture and rat lung in vivo","volume":"70","author":"Mendelsohn","year":"1982","journal-title":"J. Clin. Invest."},{"key":"10.1016\/j.bpc.2021.106565_bb0805","first-page":"Cl63","article-title":"Hormonal influence on endothelial cell angiotensin converting enzyme activity","volume":"247","author":"Krulewitz","year":"1984","journal-title":"Am. J. Phys."},{"key":"10.1016\/j.bpc.2021.106565_bb0810","doi-asserted-by":"crossref","first-page":"33","DOI":"10.1042\/bj2900033","article-title":"Angiotensin I-converting enzyme in human circulating mononuclear cells: genetic polymorphism of expression in T-lymphocytes","volume":"290","author":"Costerousse","year":"1993","journal-title":"Biochem. J."},{"key":"10.1016\/j.bpc.2021.106565_bb0815","doi-asserted-by":"crossref","first-page":"780","DOI":"10.1161\/01.RES.11.5.780","article-title":"Effect of acute sympathectomy on responses to angiotensin and norepinephrine","volume":"11","author":"Zimmerman","year":"1962","journal-title":"Circ. Res."},{"key":"10.1016\/j.bpc.2021.106565_bb0820","doi-asserted-by":"crossref","first-page":"30","DOI":"10.1016\/S0022-3565(25)26573-9","article-title":"Vascular reactivity of reserpine-pretreated dogs","volume":"141","author":"Baum","year":"1963","journal-title":"J. Pharmacol. Exp. Ther."},{"key":"10.1016\/j.bpc.2021.106565_bb0825","doi-asserted-by":"crossref","first-page":"76","DOI":"10.1007\/s001090100210","article-title":"Tissue renin-angiotensin systems: new insights from experimental animal models in hypertension research","volume":"79","author":"Bader","year":"2001","journal-title":"J. Mol. Med."},{"key":"10.1016\/j.bpc.2021.106565_bb0830","doi-asserted-by":"crossref","first-page":"469","DOI":"10.1016\/S0271-5317(04)00058-2","article-title":"Angiotensin I\u2013 converting enzyme inhibitory peptides derived from food proteins and their physiological and pharmacological effects","volume":"24","author":"Lesch","year":"2004","journal-title":"Nutr. Res."},{"issue":"9","key":"10.1016\/j.bpc.2021.106565_bb0835","doi-asserted-by":"crossref","first-page":"23","DOI":"10.1016\/j.cis.2010.11.001","article-title":"Antihypertensive peptides: production, bioavailability and incorporation into foods","volume":"165","author":"Hern\u00e1ndez-Ledesma","year":"2011","journal-title":"Adv. Colloid Interf. Sci."},{"key":"10.1016\/j.bpc.2021.106565_bb0840","doi-asserted-by":"crossref","first-page":"483","DOI":"10.1002\/med.2610050405","article-title":"Recent developments in the design of angiotensin converting enzyme inhibitors","volume":"5","author":"Wyvratt","year":"1985","journal-title":"Med. Res. Rev."},{"key":"10.1016\/j.bpc.2021.106565_bb0845","doi-asserted-by":"crossref","first-page":"112","DOI":"10.1038\/nature03712","article-title":"Angiotensin-converting enzyme 2 protects from severe acute lung failure","volume":"436","author":"Imai","year":"2005","journal-title":"Nature."},{"key":"10.1016\/j.bpc.2021.106565_bb0850","doi-asserted-by":"crossref","first-page":"441","DOI":"10.1126\/science.191908","article-title":"Design of specific inhibitors of angiotensin converting enzyme: new class of orally active antihypertensive agents","volume":"196","author":"Ondetti","year":"1977","journal-title":"Science."},{"issue":"1","key":"10.1016\/j.bpc.2021.106565_bb0855","first-page":"281","article-title":"Effect of angiotensin \u0406-converting enzyme inhibitory peptide from rice dregs protein on antihypertensive activity in spontaneously hypertensive rats","volume":"16","author":"Chen","year":"2007","journal-title":"Asia Pac. J. Clin. Nutr."},{"issue":"8","key":"10.1016\/j.bpc.2021.106565_bb0860","doi-asserted-by":"crossref","first-page":"1813","DOI":"10.1016\/j.foodhyd.2011.02.007","article-title":"Functional and bioactive properties of collagen and gelatin from alternative sources: A review","volume":"25","author":"G\u00f3mez-Guill\u00e9n","year":"2011","journal-title":"Food Hydrocoll."},{"key":"10.1016\/j.bpc.2021.106565_bb0865","doi-asserted-by":"crossref","first-page":"280","DOI":"10.1038\/288280a0","article-title":"A new class of angiotensin converting enzyme inhibitors","volume":"298","author":"Patchett","year":"1980","journal-title":"Nature"},{"key":"10.1016\/j.bpc.2021.106565_bb0870","doi-asserted-by":"crossref","first-page":"1623","DOI":"10.1161\/01.ATV.19.7.1623","article-title":"Angiotensin induces inflammatory activation of human vascular smooth muscle cells","volume":"19","author":"Kranzh\u00f6fer","year":"1999","journal-title":"Arterioscler. Thromb. Vasc. Biol."},{"key":"10.1016\/j.bpc.2021.106565_bb0875","doi-asserted-by":"crossref","first-page":"1098","DOI":"10.1056\/NEJM199104183241605","article-title":"Association of the renin-sodium profile with the risk of myocardial infarction in patients with hypertension","volume":"324","author":"Alderman","year":"1991","journal-title":"N. Engl. J. Med."},{"key":"10.1016\/j.bpc.2021.106565_bb0880","doi-asserted-by":"crossref","first-page":"616","DOI":"10.1056\/NEJM199308263290905","article-title":"Plasma renin activity and ischemic heart disease","volume":"329","author":"Meade","year":"1993","journal-title":"N. Engl. J. Med."},{"key":"10.1016\/j.bpc.2021.106565_bb0885","first-page":"1","article-title":"Plasma renin activity: a risk factor for myocardial infarction in hypertensive patients","volume":"10","author":"Alderman","year":"1997","journal-title":"J. Hypertens."},{"key":"10.1016\/j.bpc.2021.106565_bb0890","doi-asserted-by":"crossref","first-page":"484","DOI":"10.1161\/01.ATV.20.2.484","article-title":"ACE gene polymorphism in cardiovascular disease: meta-analyses of small and large studies in whites","volume":"20","author":"Agerholm-Larsen","year":"2000","journal-title":"Arterioscler. Thromb. Vasc. Biol."},{"issue":"5","key":"10.1016\/j.bpc.2021.106565_bb0895","doi-asserted-by":"crossref","first-page":"770","DOI":"10.1161\/01.CIR.58.5.770","article-title":"Angiotensin converting enzyme inhibition in patients with congestive heart failure","volume":"58","author":"Gavras","year":"1978","journal-title":"Circulation."},{"issue":"1","key":"10.1016\/j.bpc.2021.106565_bb0900","doi-asserted-by":"crossref","first-page":"1602","DOI":"10.1161\/01.CIR.88.4.1602","article-title":"Hemodynamic and neurohormonal effects of the angiotensin II antagonist losartan in patients with congestive heart failure","volume":"88","author":"Gottlieb","year":"1993","journal-title":"Circulation."},{"issue":"1","key":"10.1016\/j.bpc.2021.106565_bb0905","doi-asserted-by":"crossref","first-page":"60","DOI":"10.1016\/S0735-1097(99)00537-9","article-title":"Comparative study of ACE-inhibition, angiotensin II antagonism, and calcium channel blockade on flow-mediated vasodilation in patients with coronary disease (BANFF Study)","volume":"35","author":"Anderson","year":"2000","journal-title":"J. Am. Coll. Cardiol."},{"key":"10.1016\/j.bpc.2021.106565_bb0910","doi-asserted-by":"crossref","first-page":"351","DOI":"10.1007\/s00726-005-0289-3","article-title":"Strategies to improve plasma half life time of peptide and protein drugs","volume":"30","author":"Werle","year":"2006","journal-title":"Amino Acids"},{"key":"10.1016\/j.bpc.2021.106565_bb0915","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1136\/gut.35.3_Suppl.S1","article-title":"Somatostatin and somatostatin analogues: pharmacokinetics and pharmakodynamic effects","volume":"35","author":"Harris","year":"1994","journal-title":"Gut"},{"issue":"2","key":"10.1016\/j.bpc.2021.106565_bb0920","doi-asserted-by":"crossref","first-page":"223","DOI":"10.1016\/0014-5793(86)80816-X","article-title":"Limited proteolysis of the cellobiohydrolase I from Trichoderma reesei","volume":"204","author":"Van Tilbeurgh","year":"1986","journal-title":"FEBS"},{"key":"10.1016\/j.bpc.2021.106565_bb0925","doi-asserted-by":"crossref","first-page":"214","DOI":"10.1038\/nrd1033","article-title":"Effect of pegylation on pharmaceuticals","volume":"2","author":"Harris","year":"2003","journal-title":"Nat. Rev. Drug Discov."},{"key":"10.1016\/j.bpc.2021.106565_bb0930","doi-asserted-by":"crossref","first-page":"531","DOI":"10.1517\/14728214.2015.1113254","article-title":"What is the future of PEGylated therapies?","volume":"20","author":"Swierczewska","year":"2015","journal-title":"Expert Opin. Emerg. Drugs"},{"key":"10.1016\/j.bpc.2021.106565_bb0935","doi-asserted-by":"crossref","first-page":"1340","DOI":"10.1080\/00498250802413856","article-title":"PEGylation of somatropin (recombinant human growth hormone): Impact on its clearance in humans","volume":"38","author":"Webster","year":"2008","journal-title":"Xenobiotica."},{"key":"10.1016\/j.bpc.2021.106565_bb0940","doi-asserted-by":"crossref","first-page":"2474","DOI":"10.1002\/cmdc.201600374","article-title":"Half-life extension of biopharmaceuticals using chemical methods: Alternatives to PEGylation","volume":"11","author":"van Witteloostuijn","year":"2016","journal-title":"Chemmedchem."},{"key":"10.1016\/j.bpc.2021.106565_bb0945","doi-asserted-by":"crossref","first-page":"4932","DOI":"10.2174\/1381612825666190206105232","article-title":"Recent advances in half-life extension strategies for therapeutic peptides and proteins","volume":"24","author":"Tan","year":"2018","journal-title":"Curr.Pharm. Des."},{"key":"10.1016\/j.bpc.2021.106565_bb0950","doi-asserted-by":"crossref","first-page":"793","DOI":"10.1038\/nchembio.1907","article-title":"A biomimetic approach for enhancing the in vivo half-life of peptides","volume":"11","author":"Penchala","year":"2015","journal-title":"Nat. Chem. Biol."},{"key":"10.1016\/j.bpc.2021.106565_bb0955","doi-asserted-by":"crossref","first-page":"436","DOI":"10.1016\/j.biotechadv.2011.03.005","article-title":"Longer action means better drug: Tuning up protein therapeutics","volume":"29","author":"Szlachcic","year":"2011","journal-title":"Biotechnol. Adv."},{"key":"10.1016\/j.bpc.2021.106565_bb0960","doi-asserted-by":"crossref","first-page":"194","DOI":"10.1021\/jm00079a027","article-title":"Synthesis, stability, and biological evaluation of water-soluble prodrugs of a new echinocandin lipopeptide. Discovery of a potential clinical agent for the treatment of systemic candidiasis and pneumocystis carinii pneumonia (PCP)","volume":"35","author":"Balkovec","year":"1992","journal-title":"J. Med. Chem."},{"key":"10.1016\/j.bpc.2021.106565_bb0965","doi-asserted-by":"crossref","first-page":"521","DOI":"10.1146\/annurev.pa.33.040193.002513","article-title":"Prodrugs of peptides and proteins for improved formulation and delivery","volume":"32","author":"Oliyai","year":"1993","journal-title":"Annu. Rev. Pharmacol. Toxicol."},{"key":"10.1016\/j.bpc.2021.106565_bb0970","doi-asserted-by":"crossref","first-page":"4","DOI":"10.3390\/biom8010004","article-title":"Antimicrobial peptides: diversity, mechanism of action and strategies to improve the activity and biocompatibility in vivo","volume":"8","author":"Kumar","year":"2018","journal-title":"Biomolecules."},{"key":"10.1016\/j.bpc.2021.106565_bb0975","doi-asserted-by":"crossref","first-page":"2733","DOI":"10.1007\/s00726-014-1819-7","article-title":"Impact of fluorination on proteolytic stability of peptides: a case study with \u03b1-chymotrypsin and pepsin","volume":"46","author":"Asante","year":"2014","journal-title":"Amino Acids"},{"key":"10.1016\/j.bpc.2021.106565_bb0980","doi-asserted-by":"crossref","first-page":"106178","DOI":"10.1016\/j.bpc.2019.106178","article-title":"Albumin-bound nanodiscs as delivery vehicle candidates: development and characterization","volume":"251","author":"Damiati","year":"2019","journal-title":"Biophys. Chem."},{"key":"10.1016\/j.bpc.2021.106565_bb0985","doi-asserted-by":"crossref","first-page":"106461","DOI":"10.1016\/j.bpc.2020.106461","article-title":"Therapeutic potential of graphitic carbon nitride as a drug delivery system for cisplatin (anticancer drug): A DFT approach","volume":"267","author":"Perveen","year":"2020","journal-title":"Biophys. Chem."},{"key":"10.1016\/j.bpc.2021.106565_bb0990","doi-asserted-by":"crossref","first-page":"106407","DOI":"10.1016\/j.bpc.2020.106407","article-title":"Amino acid-functionalized borospherenes as drug delivery systems","volume":"263","author":"Zheng","year":"2020","journal-title":"Biophys. Chem."},{"key":"10.1016\/j.bpc.2021.106565_bb0995","doi-asserted-by":"crossref","first-page":"106318","DOI":"10.1016\/j.bpc.2019.106318","article-title":"Thermodynamic, viscoelastic and electrical properties of lipid membranes in the presence of astaxanthin","volume":"258","author":"Dopiera\u0142a","year":"2020","journal-title":"Biophys. Chem."},{"key":"10.1016\/j.bpc.2021.106565_bb1000","doi-asserted-by":"crossref","first-page":"106228","DOI":"10.1016\/j.bpc.2019.106228","article-title":"Apomyoglobin is an efficient carrier for zinc phthalocyanine in photodynamic therapy of tumors","volume":"253","author":"Cozzolino","year":"2019","journal-title":"Biophys. Chem."},{"key":"10.1016\/j.bpc.2021.106565_bb1005","doi-asserted-by":"crossref","first-page":"9243","DOI":"10.1021\/bi801045n","article-title":"Using fluorous amino acids to probe the effects of changing hydrophobicity on the physical and biological properties of the \u03b2-hairpin antimicrobial peptide protegrin-1","volume":"47","author":"Gottler","year":"2008","journal-title":"Biochemistry."},{"key":"10.1016\/j.bpc.2021.106565_bb1010","doi-asserted-by":"crossref","first-page":"370","DOI":"10.1002\/cbic.200700643","article-title":"Using fluorous amino acids to modulate the biological activity of an antimicrobial peptide","volume":"9","author":"Gottler","year":"2008","journal-title":"ChemBioChem."},{"issue":"2","key":"10.1016\/j.bpc.2021.106565_bb1015","doi-asserted-by":"crossref","first-page":"357","DOI":"10.1016\/j.bbamem.2007.11.008","article-title":"Studies on anticancer activities of antimicrobial peptides","volume":"1778","author":"Hoskin","year":"2008","journal-title":"Biochim. Biophys. Acta Biomembr."},{"key":"10.1016\/j.bpc.2021.106565_bb1020","doi-asserted-by":"crossref","first-page":"55","DOI":"10.1016\/S0005-2736(99)00200-X","article-title":"Mechanism of the binding, insertion and destabilization ofphospholipid bilayer membranes by alpha-helical antimicrobial and cellnon-selective membrane-lytic peptides","volume":"1462","author":"Shai","year":"1999","journal-title":"Biochim. Biophys. Acta"},{"key":"10.1016\/j.bpc.2021.106565_bb1025","doi-asserted-by":"crossref","first-page":"4278","DOI":"10.1046\/j.1432-1327.2001.02345.x","article-title":"Crumpled structure of the custom hydrophobic lytic peptide cecropin B3","volume":"268","author":"Srisailam","year":"2001","journal-title":"Eur. J. Biochem."},{"key":"10.1016\/j.bpc.2021.106565_bb1030","doi-asserted-by":"crossref","first-page":"4003","DOI":"10.1016\/S0021-9258(19)84952-9","article-title":"Determination of the disulfide array in the human defensin HNP-2: a covalently cyclized peptide","volume":"264","author":"Selsted","year":"1989","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.bpc.2021.106565_bb1035","doi-asserted-by":"crossref","first-page":"1481","DOI":"10.1126\/science.2006422","article-title":"Crystal structure of defensinHNP-3, an amphiphilic dimmer: mechanisms of membrane permeabilization","volume":"251","author":"Hill","year":"1991","journal-title":"Science."},{"key":"10.1016\/j.bpc.2021.106565_bb1040","doi-asserted-by":"crossref","first-page":"2686","DOI":"10.4049\/jimmunol.140.8.2686","article-title":"Mechanism of target cytolysis by peptide defensins. Target cell metabolic activities, possibly involving endocytosis, are crucial for expression of cytotoxicity","volume":"140","author":"Lichtenstein","year":"1988","journal-title":"J. Immunol."},{"key":"10.1016\/j.bpc.2021.106565_bb1045","doi-asserted-by":"crossref","first-page":"1407","DOI":"10.1182\/blood.V68.6.1407.1407","article-title":"In vitro tumor cell cytolysis mediated by peptide defensins of human and rabbit granulocytes","volume":"68","author":"Lichtenstein","year":"1986","journal-title":"Blood."},{"key":"10.1016\/j.bpc.2021.106565_bb1050","doi-asserted-by":"crossref","first-page":"6529","DOI":"10.1021\/bi052629q","article-title":"Deletion of all cysteines in tachyplesin I abolishes hemolytic activity and retains antimicrobial activity and lipopolysaccharide selective binding","volume":"45","author":"Ramamoorthy","year":"2006","journal-title":"Biochemistry."},{"key":"10.1016\/j.bpc.2021.106565_bb1055","doi-asserted-by":"crossref","first-page":"435","DOI":"10.1016\/S0958-1669(97)80065-1","article-title":"Therapeutic peptides and peptidomimetics","volume":"8","author":"Kieber-Emmons","year":"1997","journal-title":"Curr. Opin. Biotechnol."},{"key":"10.1016\/j.bpc.2021.106565_bb1060","doi-asserted-by":"crossref","first-page":"472","DOI":"10.1038\/nbt0496-472","article-title":"Synthetic CD4 exocyclic peptides antagonize CD4 holorecepior binding and T-cell activation","volume":"14","author":"Zhang","year":"1996","journal-title":"Nat. Biotechnol."},{"key":"10.1016\/j.bpc.2021.106565_bb1065","doi-asserted-by":"crossref","first-page":"150","DOI":"10.1038\/nbt0297-150","article-title":"Synthetic CD4 exocyclics inhibit binding of human immunodeficiency-virus type-l envelope to CD4 and virus replication in T-lymphocytes","volume":"15","author":"Zhang","year":"1997","journal-title":"Nat. Biotechnol."},{"key":"10.1016\/j.bpc.2021.106565_bb1070","doi-asserted-by":"crossref","first-page":"452","DOI":"10.1038\/35086601","article-title":"Antibacterial agents based on the cyclic D,L-\u03b1-peptide architecture","volume":"412","author":"Fernandez-Lopez","year":"2001","journal-title":"Nature"},{"key":"10.1016\/j.bpc.2021.106565_bb1075","doi-asserted-by":"crossref","first-page":"4306","DOI":"10.1021\/jm701600a","article-title":"Synthetic antimicrobial peptidomimetics with therapeutic potential","volume":"51","author":"Haug","year":"2008","journal-title":"J. Med. Chem."},{"key":"10.1016\/j.bpc.2021.106565_bb1080","doi-asserted-by":"crossref","first-page":"366","DOI":"10.3390\/ph8030366","article-title":"Peptides and peptidomimetics for antimicrobial drug design","volume":"8","author":"Mojsoska","year":"2015","journal-title":"Pharmaceuticals."},{"key":"10.1016\/j.bpc.2021.106565_bb1085","doi-asserted-by":"crossref","first-page":"2958","DOI":"10.1021\/ja003153v","article-title":"Peptoid oligomers with alpha-chiral, aromatic side chains: effects of chain length on secondary structure","volume":"123","author":"Wu","year":"2001","journal-title":"J. Am. Chem. Soc."},{"key":"10.1016\/j.bpc.2021.106565_bb1090","doi-asserted-by":"crossref","first-page":"6778","DOI":"10.1021\/ja003154n","article-title":"Peptoid oligomers with alpha-chiral, aromatic side chains: sequence requirements for the formation of stable peptoid helices","volume":"123","author":"Wu","year":"2001","journal-title":"J. Am. Chem. Soc."},{"key":"10.1016\/j.bpc.2021.106565_bb1095","doi-asserted-by":"crossref","first-page":"297","DOI":"10.3390\/ph5030297","article-title":"Heterocycles in peptidomimetics and pseudopeptides: design and synthesis","volume":"5","author":"Cerminara","year":"2012","journal-title":"Pharmaceuticals."},{"key":"10.1016\/j.bpc.2021.106565_bb1100","doi-asserted-by":"crossref","first-page":"3747","DOI":"10.1021\/jo0016834","article-title":"Design and synthesis of a conformationally restricted trans peptide isostere based on the bioactive conformations of saquinavir and nelfinavir","volume":"66","author":"Edmonds","year":"2001","journal-title":"J. Organomet. Chem."},{"key":"10.1016\/j.bpc.2021.106565_bb1105","doi-asserted-by":"crossref","first-page":"2399","DOI":"10.1002\/ejoc.201100157","article-title":"1,2,3-Triazoles in peptidomimetic chemistry","volume":"13","author":"Pedersen","year":"2011","journal-title":"Eur. J. Org. Chem."},{"key":"10.1016\/j.bpc.2021.106565_bb1110","doi-asserted-by":"crossref","first-page":"945","DOI":"10.2174\/0929867003374499","article-title":"Conformational and topographical considerations in designing agonist peptidomimetics from peptide leads","volume":"7","author":"Hruby","year":"2000","journal-title":"Curr. Med. Chem."},{"key":"10.1016\/j.bpc.2021.106565_bb1115","doi-asserted-by":"crossref","first-page":"156","DOI":"10.1039\/C2CS35284B","article-title":"Peptides and peptidomimetics that behave as low molecular weight gelators","volume":"42","author":"Tomasini","year":"2013","journal-title":"Chem. Soc. Rev."},{"key":"10.1016\/j.bpc.2021.106565_bb1120","doi-asserted-by":"crossref","first-page":"114","DOI":"10.1002\/cmdc.201100358","article-title":"Comparison of linear and cyclic peptoid oligomers as potent antimicrobial agents","volume":"7","author":"Huang","year":"2012","journal-title":"Chem Med Chem."},{"key":"10.1016\/j.bpc.2021.106565_bb1125","doi-asserted-by":"crossref","first-page":"12905","DOI":"10.1021\/acs.langmuir.6b03477","article-title":"Cyclization improves membrane permeation by antimicrobial peptoids","volume":"32","author":"Andreev","year":"2016","journal-title":"Langmuir"},{"key":"10.1016\/j.bpc.2021.106565_bb1130","doi-asserted-by":"crossref","first-page":"327","DOI":"10.2174\/187152109789760216","article-title":"Peptidomimetics and their applications in antifungal drug design","volume":"8","author":"Moradi","year":"2009","journal-title":"Anti-Infect. Agent Med. Chem."},{"key":"10.1016\/j.bpc.2021.106565_bb1135","doi-asserted-by":"crossref","first-page":"885","DOI":"10.1016\/S0022-3565(25)12947-9","article-title":"Pharmacologic characterization of CHIR 2279, an N-substituted glycine peptoid with high-affinity binding for alpha 1-adrenoceptors","volume":"277","author":"Gibbons","year":"1996","journal-title":"J. Pharmacol. Exp. Ther."},{"issue":"7","key":"10.1016\/j.bpc.2021.106565_bb1140","doi-asserted-by":"crossref","first-page":"967","DOI":"10.1158\/1541-7786.MCR-13-0611","article-title":"Tailoring peptidomimetics for targeting protein\u2013protein Interactions","volume":"12","author":"Akram","year":"2014","journal-title":"Mol. Cancer Res."},{"key":"10.1016\/j.bpc.2021.106565_bb1145","doi-asserted-by":"crossref","first-page":"2449","DOI":"10.2174\/092986706777935041","article-title":"Peptides and peptidomimetics in medicine, surgery and biotechnology","volume":"13","author":"Gentilucci","year":"2006","journal-title":"Curr. Med. Chem."},{"issue":"18","key":"10.1016\/j.bpc.2021.106565_bb1150","doi-asserted-by":"crossref","first-page":"1647","DOI":"10.4155\/fmc-2020-0180","article-title":"Evidence supporting the use of peptides and peptidomimetics as potential SARS-CoV-2 (COVID-19) therapeutics","volume":"12","author":"VanPatten","year":"2020","journal-title":"Future Med. Chem."},{"issue":"11","key":"10.1016\/j.bpc.2021.106565_bb1155","doi-asserted-by":"crossref","first-page":"1322","DOI":"10.1021\/js980082d","article-title":"Role of P-glycoprotein and cytochrome P450 3A in limiting oral absorption of peptides and peptidomimetics","volume":"87","author":"Wacher","year":"1998","journal-title":"J. Pharm. Sci."},{"key":"10.1016\/j.bpc.2021.106565_bb1160","first-page":"1131","article-title":"Anticancer gold(III) peptidomimetics: from synthesis to in vitro and ex vivo biological evaluation","author":"Boscutti","year":"2018","journal-title":"MedChemSicily."}],"container-title":["Biophysical Chemistry"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S0301462221000259?httpAccept=text\/xml","content-type":"text\/xml","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S0301462221000259?httpAccept=text\/plain","content-type":"text\/plain","content-version":"vor","intended-application":"text-mining"}],"deposited":{"date-parts":[[2025,10,4]],"date-time":"2025-10-04T07:56:15Z","timestamp":1759564575000},"score":1,"resource":{"primary":{"URL":"https:\/\/linkinghub.elsevier.com\/retrieve\/pii\/S0301462221000259"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2021,6]]},"references-count":232,"alternative-id":["S0301462221000259"],"URL":"https:\/\/doi.org\/10.1016\/j.bpc.2021.106565","relation":{},"ISSN":["0301-4622"],"issn-type":[{"value":"0301-4622","type":"print"}],"subject":[],"published":{"date-parts":[[2021,6]]},"assertion":[{"value":"Elsevier","name":"publisher","label":"This article is maintained by"},{"value":"The structural reconformation of peptides in enhancing functional and therapeutic properties: Insights into their solid state crystallizations","name":"articletitle","label":"Article Title"},{"value":"Biophysical Chemistry","name":"journaltitle","label":"Journal Title"},{"value":"https:\/\/doi.org\/10.1016\/j.bpc.2021.106565","name":"articlelink","label":"CrossRef DOI link to publisher maintained version"},{"value":"article","name":"content_type","label":"Content Type"},{"value":"\u00a9 2021 Published by Elsevier B.V.","name":"copyright","label":"Copyright"}],"article-number":"106565"}}