{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,9,3]],"date-time":"2026-09-03T10:54:17Z","timestamp":1788432857915,"version":"build-2803163510"},"reference-count":57,"publisher":"MDPI AG","issue":"3","license":[{"start":{"date-parts":[[2020,2,5]],"date-time":"2020-02-05T00:00:00Z","timestamp":1580860800000},"content-version":"vor","delay-in-days":0,"URL":"https:\/\/creativecommons.org\/licenses\/by\/4.0\/"}],"funder":[{"name":"Leading Talents of Zhongyuan Science and Technology Innovation","award":["194200510014"],"award-info":[{"award-number":["194200510014"]}]}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["IJMS"],"abstract":"<jats:p>The aim of this study was to isolate and identify angiotensin I-converting enzyme (ACE) inhibitory peptides from sesame protein through simulated gastrointestinal digestion in vitro, and to explore the underlying mechanisms by molecular docking. The sesame protein was enzymatically hydrolyzed by pepsin, trypsin, and \u03b1-chymotrypsin. The degree of hydrolysis (DH) and peptide yield increased with the increase of digest time. Moreover, ACE inhibitory activity was enhanced after digestion. The sesame protein digestive solution (SPDS) was purified by ultrafiltration through different molecular weight cut-off (MWCO) membranes and SPDS-VII (&lt; 3 kDa) had the strongest ACE inhibition. SPDS-VII was further purified by NGC Quest\u2122 10 Plus Chromatography System and finally 11 peptides were identified by Nano UHPLC-ESI-MS\/MS (nano ultra-high performance liquid chromatography-electrospray ionization mass spectrometry\/mass spectrometry) from peak 4. The peptide GHIITVAR from 11S globulin displayed the strongest ACE inhibitory activity (IC50 = 3.60 \u00b1 0.10 \u03bcM). Furthermore, the docking analysis revealed that the ACE inhibition of GHIITVAR was mainly attributed to forming very strong hydrogen bonds with the active sites of ACE. These results identify sesame protein as a rich source of ACE inhibitory peptides and further indicate that GHIITVAR has the potential for development of new functional foods.<\/jats:p>","DOI":"10.3390\/ijms21031059","type":"journal-article","created":{"date-parts":[[2020,2,6]],"date-time":"2020-02-06T02:59:18Z","timestamp":1580957958000},"page":"1059","update-policy":"https:\/\/doi.org\/10.3390\/mdpi_crossmark_policy","source":"Crossref","is-referenced-by-count":85,"title":["Novel ACE Inhibitory Peptides Derived from Simulated Gastrointestinal Digestion in Vitro of Sesame (Sesamum indicum L.) Protein and Molecular Docking Study"],"prefix":"10.3390","volume":"21","author":[{"given":"Ruidan","family":"Wang","sequence":"first","affiliation":[{"name":"Research Center for Agricultural and Sideline Products Processing, Henan Academy of Agricultural Sciences, Zhengzhou 450002, China"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Xin","family":"Lu","sequence":"additional","affiliation":[{"name":"Research Center for Agricultural and Sideline Products Processing, Henan Academy of Agricultural Sciences, Zhengzhou 450002, China"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Qiang","family":"Sun","sequence":"additional","affiliation":[{"name":"Research Center for Agricultural and Sideline Products Processing, Henan Academy of Agricultural Sciences, Zhengzhou 450002, China"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Jinhong","family":"Gao","sequence":"additional","affiliation":[{"name":"Research Center for Agricultural and Sideline Products Processing, Henan Academy of Agricultural Sciences, Zhengzhou 450002, China"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Lin","family":"Ma","sequence":"additional","affiliation":[{"name":"Research Center for Agricultural and Sideline Products Processing, Henan Academy of Agricultural Sciences, Zhengzhou 450002, China"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-1661-1178","authenticated-orcid":false,"given":"Jinian","family":"Huang","sequence":"additional","affiliation":[{"name":"Research Center for Agricultural and Sideline Products Processing, Henan Academy of Agricultural Sciences, Zhengzhou 450002, China"}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"1968","published-online":{"date-parts":[[2020,2,5]]},"reference":[{"key":"ref_1","first-page":"S3","article-title":"Epidemiology and risk of hypertension in the elderly: The Framingham-Study","volume":"6","author":"Vokonas","year":"1988","journal-title":"J. Hypertens Suppl."},{"key":"ref_2","doi-asserted-by":"crossref","unstructured":"Global Burden of Metabolic Risk Factors for Chronic Diseases Collaboration (2014). Cardiovascular disease, chronic kidney disease, and diabetes mortality burden of cardiometabolic risk factors from 1980 to 2010: A comparative risk assessment. Lancet Diabetes Endocrinol., 2, 634\u2013647.","DOI":"10.1016\/S2213-8587(14)70102-0"},{"key":"ref_3","doi-asserted-by":"crossref","first-page":"1903","DOI":"10.1016\/S0140-6736(02)11911-8","article-title":"Prospective Studies Collaboration. Age-specific relevance of usual blood pressure to vascular mortality: A meta-analysis of individual data for one million adults in 61 prospective studies","volume":"360","author":"Lewington","year":"2002","journal-title":"Lancet"},{"key":"ref_4","doi-asserted-by":"crossref","first-page":"92","DOI":"10.1016\/j.jcs.2014.01.019","article-title":"Potential angiotensin I converting enzyme inhibitory peptides from gluten hydrolysate: Biochemical characterization and molecular docking study","volume":"60","author":"Asoodeh","year":"2014","journal-title":"J. Cereal Sci."},{"key":"ref_5","first-page":"273","article-title":"Bioactive peptides and hydrolysates from pulses and their potential use as functional ingredients","volume":"79","year":"2014","journal-title":"J. Food Sci."},{"key":"ref_6","doi-asserted-by":"crossref","first-page":"9234","DOI":"10.1021\/jf9018245","article-title":"Angiotensin-I converting enzyme inhibitory activity of hydrolysates from oat (Avena Sativa) proteins by in silico and in vitro analyses","volume":"57","author":"Cheung","year":"2009","journal-title":"J Agric Food Chem."},{"key":"ref_7","doi-asserted-by":"crossref","first-page":"2682","DOI":"10.1016\/j.foodchem.2013.04.064","article-title":"LC-MS\/MS coupled with QSAR modeling in characterising of angiotensin I-converting enzyme inhibitory peptides from soybean proteins","volume":"141","author":"Gu","year":"2013","journal-title":"Food Chem."},{"key":"ref_8","doi-asserted-by":"crossref","first-page":"945","DOI":"10.1016\/j.idairyj.2005.10.012","article-title":"Bioactive peptides: Production and functionality","volume":"16","author":"Korhonen","year":"2006","journal-title":"Int. Dairy J."},{"key":"ref_9","doi-asserted-by":"crossref","first-page":"171","DOI":"10.1007\/s00394-008-0710-2","article-title":"Bioactive peptides and protein from foods: Indication for health effects","volume":"47","author":"Moller","year":"2008","journal-title":"Eur J. Nutr."},{"key":"ref_10","doi-asserted-by":"crossref","first-page":"311","DOI":"10.1016\/j.foodhyd.2018.06.048","article-title":"Purification and characterization of antioxidative peptides derived from chicken skin gelatin hydrolysate","volume":"85","author":"Sarbon","year":"2018","journal-title":"Food Hydrocoll."},{"key":"ref_11","doi-asserted-by":"crossref","first-page":"685","DOI":"10.1007\/s00217-015-2576-x","article-title":"Isolation and characterization of an antibacterial peptide from protein hydrolysates of Spirulina platensis","volume":"242","author":"Sun","year":"2016","journal-title":"Eur Food Res Technol."},{"key":"ref_12","doi-asserted-by":"crossref","first-page":"1909","DOI":"10.1016\/j.jff.2013.09.012","article-title":"Inhibition of dipeptidyl peptidase IV (DPP-IV) by proline containing casein-derived peptides","volume":"5","author":"Nongonierma","year":"2013","journal-title":"J. Funct Foods."},{"key":"ref_13","doi-asserted-by":"crossref","first-page":"65","DOI":"10.1016\/j.jff.2016.07.006","article-title":"Isolation and characterization of angiotensin I-converting enzyme (ACE) inhibitory peptides from Ulva rigida C. Agardh protein hydrolysate","volume":"26","author":"Paiva","year":"2016","journal-title":"J. Funct Foods."},{"key":"ref_14","doi-asserted-by":"crossref","first-page":"83","DOI":"10.1016\/j.bcab.2017.06.008","article-title":"Exploration of potential angiotensin converting enzyme inhibitory peptides generated from enzymatic hydrolysis of goat milk proteins","volume":"11","author":"Rani","year":"2017","journal-title":"Biocatal. Agric. Biotechnol."},{"key":"ref_15","doi-asserted-by":"crossref","first-page":"212","DOI":"10.1016\/j.ifset.2013.02.002","article-title":"Identification of a novel angiotensin-I converting enzyme inhibitory peptide from ostrich egg white and studying its interactions with the enzyme","volume":"18","author":"Tanzadehpanah","year":"2013","journal-title":"Innov. Food Sci. Emerg. Technol."},{"key":"ref_16","doi-asserted-by":"crossref","first-page":"738","DOI":"10.1007\/s12010-012-0024-y","article-title":"Review on the angiotensin-I-converting enzyme (ACE) inhibitor peptides from marine proteins","volume":"169","author":"He","year":"2013","journal-title":"Appl. Biochem. Biotechnol."},{"key":"ref_17","first-page":"159","article-title":"Nutritional, medicinal and industrial uses of sesame (Sesamum indicum L.) seeds\u2014An overview","volume":"75","author":"Anilakumar","year":"2010","journal-title":"Agric. Conspec. Sci."},{"key":"ref_18","doi-asserted-by":"crossref","first-page":"191","DOI":"10.1016\/j.foodchem.2015.10.094","article-title":"Some microbial, chemical and sensorial properties of gamma irradiated sesame (Sesamum indicum L.) seeds","volume":"197","year":"2016","journal-title":"Food Chem."},{"key":"ref_19","doi-asserted-by":"crossref","first-page":"1118","DOI":"10.1271\/bbb.70.1118","article-title":"Antihypertensive effect of angiotensin I-converting enzyme inhibitory peptides from a sesame protein hydrolysate in spontaneously hypertensive rats","volume":"70","author":"Nakano","year":"2006","journal-title":"Biosci. Biotechnol. Biochem."},{"key":"ref_20","doi-asserted-by":"crossref","first-page":"433","DOI":"10.1007\/s10989-015-9471-y","article-title":"Purification and identification of a novel angiotensin I-converting enzyme inhibitory peptide from sesame meal","volume":"21","author":"Liu","year":"2015","journal-title":"Int. J. Pept. Res. Ther."},{"key":"ref_21","doi-asserted-by":"crossref","first-page":"108881","DOI":"10.1016\/j.lwt.2019.108881","article-title":"Analysis of protein profiles and peptides during in vitro gastrointestinal digestion of four Chinese dry-cured hams","volume":"120","author":"Jiang","year":"2020","journal-title":"LWT-Food Sci. Technol."},{"key":"ref_22","doi-asserted-by":"crossref","first-page":"12836","DOI":"10.3390\/molecules171112836","article-title":"Purification and identification of antioxidant peptides from enzymatic hydrolysates of Tilapia (Oreochromis niloticus) frame protein","volume":"17","author":"Fan","year":"2012","journal-title":"Molecules"},{"key":"ref_23","doi-asserted-by":"crossref","first-page":"696","DOI":"10.1016\/j.jfda.2017.07.008","article-title":"Production of antioxidant and ACE-inhibitory peptides from Kluyveromyces marxianus protein hydrolysates: Purification and molecular docking","volume":"26","author":"Mirzaei","year":"2018","journal-title":"J. Food Drug Anal."},{"key":"ref_24","doi-asserted-by":"crossref","first-page":"25","DOI":"10.1016\/j.seppur.2016.05.023","article-title":"Stirring-assisted dead-end ultrafiltration for protein and polyphenol recovery from purple sweet potato juices: Filtration behavior investigation and HPLC-DAD-ESI-MS2 profiling","volume":"169","author":"Zhu","year":"2016","journal-title":"Sep. Purif. Technol."},{"key":"ref_25","doi-asserted-by":"crossref","first-page":"34","DOI":"10.1016\/j.foodchem.2013.07.076","article-title":"ACE-inhibitory activity of enzymatic protein hydrolysates from Lupin and other Legumes","volume":"145","author":"Boschin","year":"2014","journal-title":"Food Chem."},{"key":"ref_26","doi-asserted-by":"crossref","first-page":"54","DOI":"10.1016\/j.lwt.2019.04.053","article-title":"Novel angiotensin-converting enzyme inhibitory peptides derived from Trichiurus lepturus myosin: Molecular docking and surface plasmon resonance study","volume":"110","author":"Fu","year":"2019","journal-title":"LWT-Food Sci. Technol."},{"key":"ref_27","doi-asserted-by":"crossref","first-page":"266","DOI":"10.1016\/j.jff.2017.03.008","article-title":"Novel angiotensin I-converting enzyme inhibitory peptides from protease hydrolysates of Qula casein: Quantitative structure-activity relationship modeling and molecular docking study","volume":"32","author":"Lin","year":"2017","journal-title":"J. Funct. Foods."},{"key":"ref_28","doi-asserted-by":"crossref","first-page":"360","DOI":"10.1016\/j.foodres.2012.01.001","article-title":"Sesame protein isolate: Fractionation; secondary structure and functional properties","volume":"46","author":"Achouri","year":"2012","journal-title":"Food Res. Int."},{"key":"ref_29","doi-asserted-by":"crossref","first-page":"707","DOI":"10.1016\/j.foodres.2018.09.001","article-title":"Extraction; identification and structure-activity relationship of antioxidant peptides from sesame (Sesamum indicum L.) protein hydrolysate","volume":"116","author":"Lu","year":"2019","journal-title":"Food Res. Int."},{"key":"ref_30","doi-asserted-by":"crossref","first-page":"430","DOI":"10.1016\/j.lwt.2017.03.004","article-title":"Isolation and characterization of nutraceutically potential ACE-Inhibitory peptides from leatherjacket (Meuchenia sp.) protein hydrolysates","volume":"80","author":"Salampessy","year":"2017","journal-title":"LWT-Food Sci. Technol."},{"key":"ref_31","doi-asserted-by":"crossref","first-page":"2240","DOI":"10.1016\/j.procbio.2012.08.019","article-title":"Angiotensin I converting enzyme (ACE) inhibitory peptides from salmon byproduct protein hydrolysate by alcalase hydrolysis","volume":"47","author":"Ahn","year":"2012","journal-title":"Process Biochem."},{"key":"ref_32","doi-asserted-by":"crossref","first-page":"190","DOI":"10.1016\/j.foodchem.2016.09.183","article-title":"Bioavailability of angiotensin I-converting enzyme (ACE) inhibitory peptides derived from Virgibacillus halodenitrificans SK1\u20133-7 proteinases hydrolyzed tilapia muscle proteins","volume":"220","author":"Toopcham","year":"2017","journal-title":"Food Chem."},{"key":"ref_33","doi-asserted-by":"crossref","first-page":"765","DOI":"10.3390\/nu3090765","article-title":"Bioactive peptides from muscle sources: Meat and fish","volume":"3","author":"Ryan","year":"2011","journal-title":"Nutrients"},{"key":"ref_34","doi-asserted-by":"crossref","first-page":"961","DOI":"10.3168\/jds.2018-14899","article-title":"Production and transepithelial transportation of angiotensin-I-converting enzyme (ACE)-inhibitory peptides from whey protein hydrolyzed by immobilized Lactobacillus helveticus proteinase","volume":"102","author":"Guo","year":"2019","journal-title":"J. Dairy Sci."},{"key":"ref_35","doi-asserted-by":"crossref","first-page":"276","DOI":"10.1016\/j.jff.2015.10.025","article-title":"Purification and characterization of angiotensin converting enzyme-inhibitory peptides derived from Stichopus horrens: Stability study against the ACE and inhibition kinetics","volume":"20","author":"Forghani","year":"2016","journal-title":"J. Funct. Foods"},{"key":"ref_36","doi-asserted-by":"crossref","first-page":"180","DOI":"10.1016\/j.procbio.2016.12.023","article-title":"Purification and molecular docking study of angiotensin I-converting enzyme (ACE) inhibitory peptides from hydrolysates of marine sponge Stylotella aurantium","volume":"54","author":"Ko","year":"2017","journal-title":"Process Biochem."},{"key":"ref_37","doi-asserted-by":"crossref","first-page":"716","DOI":"10.1016\/j.jff.2015.02.037","article-title":"Functional and potential therapeutic ACE-inhibitory peptides derived from bromelain hydrolysis of trevally proteins","volume":"14","author":"Salampessy","year":"2015","journal-title":"J. Funct. Foods."},{"key":"ref_38","doi-asserted-by":"crossref","first-page":"632","DOI":"10.1016\/j.jff.2015.06.016","article-title":"In silico investigation of action mechanism of four novel angiotensin-I converting enzyme inhibitory peptides modified with Trp","volume":"17","author":"Xie","year":"2015","journal-title":"J. Funct. Foods"},{"key":"ref_39","doi-asserted-by":"crossref","first-page":"93","DOI":"10.1016\/j.lwt.2016.08.047","article-title":"A novel antioxidant and ACE inhibitory peptide from rice bran protein: Biochemical characterization and molecular docking study","volume":"75","author":"Wang","year":"2017","journal-title":"LWT-Food Sci. Technol."},{"key":"ref_40","doi-asserted-by":"crossref","first-page":"647","DOI":"10.1016\/j.bioorg.2019.03.057","article-title":"In vitro and in silico studies of novel synthetic ACE-inhibitory peptides derived from Saccharomyces cerevisiae protein hydrolysate","volume":"87","author":"Mirzaei","year":"2019","journal-title":"Bioorg. Chem."},{"key":"ref_41","doi-asserted-by":"crossref","first-page":"145","DOI":"10.1016\/j.procbio.2017.04.032","article-title":"In silico analysis and antihypertensive effect of ACE-inhibitory peptides from smooth-hound viscera protein hydrolysate: Enzyme-peptide interaction study using molecular docking simulation","volume":"58","author":"Abdelhedi","year":"2017","journal-title":"Process Biochem."},{"key":"ref_42","doi-asserted-by":"crossref","unstructured":"Wang, C., Tu, M., Wu, D., Chen, H., Chen, C., Wang, Z., and Jiang, L. (2018). Identification of an ACE-Inhibitory peptide from walnut protein and its evaluation of the inhibitory mechanism. Int. J. Mol. Sci., 19.","DOI":"10.3390\/ijms19041156"},{"key":"ref_43","doi-asserted-by":"crossref","first-page":"424","DOI":"10.1016\/j.jprot.2015.08.018","article-title":"Screening, discovery, and characterization of angiotensin-I converting enzyme inhibitory peptides derived from proteolytic hydrolysate of bitter melon seed proteins","volume":"128","author":"Priyanto","year":"2015","journal-title":"J. Proteomics."},{"key":"ref_44","doi-asserted-by":"crossref","first-page":"224","DOI":"10.1016\/j.foodchem.2014.08.116","article-title":"High-pressure improves enzymatic proteolysis and the release of peptides with angiotensin I converting enzyme inhibitory and antioxidant activities from lentil proteins","volume":"171","author":"Frias","year":"2015","journal-title":"Food Chem."},{"key":"ref_45","doi-asserted-by":"crossref","first-page":"7147","DOI":"10.1021\/acs.jafc.9b01071","article-title":"Identification and characterization of gastrointestinal-resistant angiotensin-converting enzyme inhibitory peptides from egg white proteins","volume":"67","author":"Fan","year":"2019","journal-title":"J. Agric. Food Chem."},{"key":"ref_46","doi-asserted-by":"crossref","first-page":"464","DOI":"10.1016\/j.foodchem.2016.10.087","article-title":"Identification, functional gastrointestinal stability and molecular docking studies of lentil peptides with dual antioxidant and Angiotensin I converting enzyme inhibitory activities","volume":"221","author":"Bonache","year":"2017","journal-title":"Food chem."},{"key":"ref_47","doi-asserted-by":"crossref","first-page":"659","DOI":"10.1016\/j.ijbiomac.2018.10.122","article-title":"A new functional protein-polysaccharide conjugate based on protein concentrate from sesame processing by-products: Functional and physico-chemical properties","volume":"122","author":"Saatchi","year":"2019","journal-title":"Int. J. Biol Macromol."},{"key":"ref_48","doi-asserted-by":"crossref","first-page":"77","DOI":"10.1016\/j.jff.2016.12.005","article-title":"Angiotensin converting enzyme (ACE) inhibitory peptides derived from the simulated in vitro gastrointestinal digestion of cooked chicken breast","volume":"29","author":"Sangsawad","year":"2017","journal-title":"J. Funct. Foods"},{"key":"ref_49","doi-asserted-by":"crossref","first-page":"2808","DOI":"10.1093\/bioinformatics\/btt484","article-title":"A fast Peptide Match service for UniProt Knowledgebase","volume":"29","author":"Chen","year":"2013","journal-title":"Bioinformatics"},{"key":"ref_50","doi-asserted-by":"crossref","first-page":"1256","DOI":"10.1021\/jf60226a042","article-title":"Determination of the degree of hydrolysis of food protein hydrolysates by trinitrobenzene sulfonic acid","volume":"27","year":"1979","journal-title":"J. Agric. Food Chem."},{"key":"ref_51","doi-asserted-by":"crossref","first-page":"70","DOI":"10.1016\/j.fbp.2015.01.007","article-title":"Enzymatic modification of sesame seed protein, sourced from waste resource for nutraceutical application","volume":"94","author":"Chatterjee","year":"2015","journal-title":"Food Bioprod. Process."},{"key":"ref_52","doi-asserted-by":"crossref","first-page":"1019","DOI":"10.1016\/S0039-9140(02)00136-4","article-title":"Comparison of the Kjeldahl method and a combustion method for total nitrogen determination in animal feed","volume":"57","author":"Rubio","year":"2002","journal-title":"Talanta"},{"key":"ref_53","doi-asserted-by":"crossref","first-page":"365","DOI":"10.1016\/j.foodchem.2016.02.127","article-title":"Isolation; purification and characterization of antioxidative peptide of pearl millet (Pennisetum glaucum) protein hydrolysate","volume":"204","author":"Agrawal","year":"2016","journal-title":"Food Chem."},{"key":"ref_54","doi-asserted-by":"crossref","first-page":"512","DOI":"10.1080\/10942910802688176","article-title":"Changes in angiotensin I-converting enzyme inhibitory activities during the ripening of douchi (a Chinese traditional soybean product) fermented by various starter cultures","volume":"13","author":"Li","year":"2010","journal-title":"Int. J. Food Prop."},{"key":"ref_55","doi-asserted-by":"crossref","first-page":"499","DOI":"10.1021\/jm020406h","article-title":"Surflex: Fully automatic flexible molecular docking using a molecular similarity-based search engine","volume":"46","author":"Jain","year":"2003","journal-title":"J. Med. Chem."},{"key":"ref_56","doi-asserted-by":"crossref","first-page":"427","DOI":"10.1007\/BF00124474","article-title":"Scoring noncovalent protein-ligand interactions: A continuous differentiable function tuned to compute binding affinities","volume":"10","author":"Jain","year":"1996","journal-title":"J. Comput. Aided Mol. Design"},{"key":"ref_57","doi-asserted-by":"crossref","first-page":"103428","DOI":"10.1016\/j.bioorg.2019.103428","article-title":"Molecular docking, antiproliferative and anticonvulsant activities of swertiamarin isolated from Enicostemma axillare","volume":"94","author":"Vaijanathappa","year":"2020","journal-title":"Bioorg. Chem."}],"container-title":["International Journal of Molecular Sciences"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/www.mdpi.com\/1422-0067\/21\/3\/1059\/pdf","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2025,10,11]],"date-time":"2025-10-11T08:55:03Z","timestamp":1760172903000},"score":1,"resource":{"primary":{"URL":"https:\/\/www.mdpi.com\/1422-0067\/21\/3\/1059"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2020,2,5]]},"references-count":57,"journal-issue":{"issue":"3","published-online":{"date-parts":[[2020,2]]}},"alternative-id":["ijms21031059"],"URL":"https:\/\/doi.org\/10.3390\/ijms21031059","relation":{},"ISSN":["1422-0067"],"issn-type":[{"value":"1422-0067","type":"electronic"}],"subject":[],"published":{"date-parts":[[2020,2,5]]}}}