{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,9,28]],"date-time":"2026-09-28T18:20:39Z","timestamp":1790619639641,"version":"4.1.0"},"reference-count":54,"publisher":"MDPI AG","issue":"12","license":[{"start":{"date-parts":[[2021,11,23]],"date-time":"2021-11-23T00:00:00Z","timestamp":1637625600000},"content-version":"vor","delay-in-days":0,"URL":"https:\/\/creativecommons.org\/licenses\/by\/4.0\/"}],"funder":[{"name":"the National Key Research and Development Program of China","award":["2018YFD0901102"],"award-info":[{"award-number":["2018YFD0901102"]}]},{"name":"the Special Funds of Fujian Ocean and Fisheries Structure Adjustment","award":["2020HYJG06"],"award-info":[{"award-number":["2020HYJG06"]}]}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["Marine Drugs"],"abstract":"<jats:p>Alcalase, neutral protease, and pepsin were used to hydrolyze the skin of Takifugu flavidus. The T. flavidus hydrolysates (TFHs) with the maximum degree of hydrolysis (DH) and angiotensin-I-converting enzyme (ACE)-inhibitory activity were selected and then ultra-filtered to obtain fractions with components of different molecular weights (MWs) (&lt;1, 1\u20133, 3\u201310, 10\u201350, and &gt;50 kDa). The components with MWs &lt; 1 kDa showed the strongest ACE-inhibitory activity with a half-maximal inhibitory concentration (IC50) of 0.58 mg\/mL. Purification and identification using semi-preparative liquid chromatography, Sephadex G-15 gel chromatography, RP-HPLC, and LC\u2013MS\/MS yielded one new potential ACE-inhibitory peptide, PPLLFAAL (non-competitive suppression mode; IC50 of 28 \u03bcmmol\u00b7L\u22121). Molecular docking and molecular dynamics simulations indicated that the peptides should bind well to ACE and interact with amino acid residues and the zinc ion at the ACE active site. Furthermore, a short-term assay of antihypertensive activity in spontaneously hypertensive rats (SHRs) revealed that PPLLFAAL could significantly decrease the systolic blood pressure (SBP) and diastolic blood pressure (DBP) of SHRs after intravenous administration. These results suggested that PPLLFAAL may have potential applications in functional foods or pharmaceuticals as an antihypertensive agent.<\/jats:p>","DOI":"10.3390\/md19120651","type":"journal-article","created":{"date-parts":[[2021,12,1]],"date-time":"2021-12-01T01:43:22Z","timestamp":1638323002000},"page":"651","update-policy":"https:\/\/doi.org\/10.3390\/mdpi_crossmark_policy","source":"Crossref","is-referenced-by-count":37,"title":["A Novel Angiotensin-I-Converting Enzyme (ACE) Inhibitory Peptide from Takifugu flavidus"],"prefix":"10.3390","volume":"19","author":[{"given":"Yongchang","family":"Su","sequence":"first","affiliation":[{"name":"College of Chemical Engineering, Huaqiao University, Xiamen 361021, China"},{"name":"Key Laboratory of Cultivation and High-Value Utilization of Marine Organisms in Fujian Province, Fisheries Research Institute of Fujian, Xiamen 361013, China"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0001-6094-5514","authenticated-orcid":false,"given":"Shicheng","family":"Chen","sequence":"additional","affiliation":[{"name":"Department of Clinical and Diagnostic Sciences, School of Health Sciences, Oakland University, 433 Meadowbrook Road, Rochester, MI 48309, USA"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Shuilin","family":"Cai","sequence":"additional","affiliation":[{"name":"College of Chemical Engineering, Huaqiao University, Xiamen 361021, China"},{"name":"Key Laboratory of Cultivation and High-Value Utilization of Marine Organisms in Fujian Province, Fisheries Research Institute of Fujian, Xiamen 361013, China"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Shuji","family":"Liu","sequence":"additional","affiliation":[{"name":"Key Laboratory of Cultivation and High-Value Utilization of Marine Organisms in Fujian Province, Fisheries Research Institute of Fujian, Xiamen 361013, China"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0001-6182-6058","authenticated-orcid":false,"given":"Nan","family":"Pan","sequence":"additional","affiliation":[{"name":"Key Laboratory of Cultivation and High-Value Utilization of Marine Organisms in Fujian Province, Fisheries Research Institute of Fujian, Xiamen 361013, China"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Jie","family":"Su","sequence":"additional","affiliation":[{"name":"Key Laboratory of Cultivation and High-Value Utilization of Marine Organisms in Fujian Province, Fisheries Research Institute of Fujian, Xiamen 361013, China"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-2372-2837","authenticated-orcid":false,"given":"Kun","family":"Qiao","sequence":"additional","affiliation":[{"name":"Key Laboratory of Cultivation and High-Value Utilization of Marine Organisms in Fujian Province, Fisheries Research Institute of Fujian, Xiamen 361013, China"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Min","family":"Xu","sequence":"additional","affiliation":[{"name":"Key Laboratory of Cultivation and High-Value Utilization of Marine Organisms in Fujian Province, Fisheries Research Institute of Fujian, Xiamen 361013, China"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Bei","family":"Chen","sequence":"additional","affiliation":[{"name":"Key Laboratory of Cultivation and High-Value Utilization of Marine Organisms in Fujian Province, Fisheries Research Institute of Fujian, Xiamen 361013, China"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-0985-8287","authenticated-orcid":false,"given":"Suping","family":"Yang","sequence":"additional","affiliation":[{"name":"College of Chemical Engineering, Huaqiao University, Xiamen 361021, China"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Zhiyu","family":"Liu","sequence":"additional","affiliation":[{"name":"Key Laboratory of Cultivation and High-Value Utilization of Marine Organisms in Fujian Province, Fisheries Research Institute of Fujian, Xiamen 361013, China"}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"1968","published-online":{"date-parts":[[2021,11,23]]},"reference":[{"key":"ref_1","first-page":"617","article-title":"Hypertension, cardiovascular diseases and defense mechanisms","volume":"128","year":"1989","journal-title":"Cas. Lek. Ceskych."},{"key":"ref_2","doi-asserted-by":"crossref","unstructured":"Daskaya-Dikmen, C., Yucetepe, A., Karbancioglu-Guler, F., Daskaya, H., and Ozcelik, B. (2017). Angiotensin-I-converting enzyme (ACE)-inhibitory peptides from plants. Nutrients, 9.","DOI":"10.3390\/nu9040316"},{"key":"ref_3","doi-asserted-by":"crossref","first-page":"938","DOI":"10.1136\/jcp.36.8.938","article-title":"Angiotensin-converting enzyme and its clinical significance\u2014A review","volume":"36","author":"Studdy","year":"1983","journal-title":"J. Clin. Pathol."},{"key":"ref_4","doi-asserted-by":"crossref","first-page":"235","DOI":"10.1146\/annurev-food-022814-015520","article-title":"Antihypertensive peptides from food proteins","volume":"6","author":"Aluko","year":"2015","journal-title":"Annu. Rev. Food Sci. Technol."},{"key":"ref_5","doi-asserted-by":"crossref","unstructured":"Abachi, S., Bazinet, L., and Beaulieu, L. (2019). Antihypertensive and angiotensin-I-converting enzyme (ACE)-inhibitory peptides from fish as potential cardioprotective compounds. Mar. Drugs, 17.","DOI":"10.3390\/md17110613"},{"key":"ref_6","doi-asserted-by":"crossref","first-page":"1559","DOI":"10.1185\/030079904X4185","article-title":"Provision of cardiovascular protection by ACE inhibitors: A review of recent trials","volume":"20","author":"Bertrand","year":"2004","journal-title":"Curr. Med. Res. Opin."},{"key":"ref_7","doi-asserted-by":"crossref","first-page":"214","DOI":"10.1016\/j.tifs.2017.07.011","article-title":"Revisiting the mechanisms of ACE inhibitory peptides from food proteins","volume":"69","author":"Wu","year":"2017","journal-title":"Trends Food Sci. Technol."},{"key":"ref_8","doi-asserted-by":"crossref","first-page":"S33","DOI":"10.1017\/S0007114500002221","article-title":"Milk protein-derived peptide inhibitors of angiotensin-I-converting enzyme","volume":"84","author":"FitzGerald","year":"2000","journal-title":"Br. J. Nutr."},{"key":"ref_9","doi-asserted-by":"crossref","first-page":"1080","DOI":"10.3390\/md8041080","article-title":"Angiotensin-I-converting enzyme (ACE) inhibitors from marine resources: Prospects in the pharmaceutical industry","volume":"8","author":"Wijesekara","year":"2010","journal-title":"Mar. Drugs"},{"key":"ref_10","doi-asserted-by":"crossref","first-page":"3536","DOI":"10.1002\/jsfa.7538","article-title":"Angiotensin converting enzyme (ACE) inhibitory and antihypertensive activities of protein hydrolysate from meat of Kacang goat (Capra aegagrus hircus)","volume":"96","author":"Mirdhayati","year":"2016","journal-title":"J. Sci. Food Agric."},{"key":"ref_11","doi-asserted-by":"crossref","first-page":"19","DOI":"10.1016\/j.foodchem.2016.12.039","article-title":"Identification and quantification of ACE-inhibiting peptides in enzymatic hydrolysates of plant proteins","volume":"224","author":"Rudolph","year":"2017","journal-title":"Food Chem."},{"key":"ref_12","doi-asserted-by":"crossref","first-page":"8106","DOI":"10.1021\/jf0508908","article-title":"ACE Inhibitory peptides derived from enzymatic hydrolysates of animal muscle protein: A review","volume":"53","author":"Vercruysse","year":"2005","journal-title":"J. Agric. Food Chem."},{"key":"ref_13","doi-asserted-by":"crossref","first-page":"350","DOI":"10.1039\/c2fo10192k","article-title":"Antihypertensive peptides from food proteins: A review","volume":"3","author":"Miralles","year":"2012","journal-title":"Food Funct."},{"key":"ref_14","doi-asserted-by":"crossref","first-page":"1770","DOI":"10.1016\/j.foodchem.2011.06.051","article-title":"Purification and identification of ACE inhibitory peptides from Haruan (Channa striatus) myofibrillar protein hydrolysate using HPLC\u2013ESI-TOF MS\/MS","volume":"129","author":"Ghassem","year":"2011","journal-title":"Food Chem."},{"key":"ref_15","doi-asserted-by":"crossref","first-page":"3240","DOI":"10.1002\/jsfa.7507","article-title":"Production of the angiotensin I converting enzyme inhibitory peptides and isolation of four novel peptides from jellyfish (Rhopilema esculentum) protein hydrolysate","volume":"96","author":"Liu","year":"2016","journal-title":"J. Sci. Food Agric."},{"key":"ref_16","doi-asserted-by":"crossref","first-page":"457","DOI":"10.1016\/j.procbio.2008.01.018","article-title":"Purification and identification of novel angiotensin-I-converting enzyme inhibitory peptides from shark meat hydrolysate","volume":"43","author":"Wu","year":"2008","journal-title":"Process Biochem."},{"key":"ref_17","doi-asserted-by":"crossref","first-page":"96","DOI":"10.1016\/j.foodchem.2009.04.086","article-title":"A novel angiotensin I converting enzyme inhibitory peptide from tuna frame protein hydrolysate and its antihypertensive effect in spontaneously hypertensive rats","volume":"118","author":"Lee","year":"2010","journal-title":"Food Chem."},{"key":"ref_18","doi-asserted-by":"crossref","first-page":"71","DOI":"10.1016\/j.aquaculture.2010.02.005","article-title":"Effects of salinity on embryos and larvae of tawny puffer Takifugu flavidus","volume":"302","author":"Zhang","year":"2010","journal-title":"Aquaculture"},{"key":"ref_19","doi-asserted-by":"crossref","first-page":"627","DOI":"10.1093\/dnares\/dsu025","article-title":"Draft sequencing and analysis of the genome of pufferfish Takifugu flavidus","volume":"21","author":"Gao","year":"2014","journal-title":"DNA Res."},{"key":"ref_20","doi-asserted-by":"crossref","unstructured":"Chen, J., Li, M., Yi, R., Bai, K., Wang, G., Tan, R., Sun, S., and Xu, N. (2019). Electrodialysis extraction of Pufferfish skin (Takifugu flavidus): A promising source of collagen. Mar. Drugs, 17.","DOI":"10.3390\/md17010025"},{"key":"ref_21","doi-asserted-by":"crossref","unstructured":"Sun, S., Xu, X., Sun, X., Zhang, X., Chen, X., and Xu, N. (2019). Preparation and identification of ACE inhibitory peptides from the marine macroalga Ulva intestinalis. Mar. Drugs, 17.","DOI":"10.3390\/md17030179"},{"key":"ref_22","first-page":"525","article-title":"Characteristics and use of protein hydrolysates (review)","volume":"36","author":"Nekliudov","year":"2000","journal-title":"Prikl. Biokhimiia Mikrobiol."},{"key":"ref_23","doi-asserted-by":"crossref","first-page":"109","DOI":"10.1016\/bs.afnr.2016.10.003","article-title":"Protein hydrolysates and biopeptides: Production, biological activities, and applications in foods and health benefits. A review","volume":"81","author":"Nasri","year":"2017","journal-title":"Adv. Food Nutr. Res."},{"key":"ref_24","first-page":"466","article-title":"Production of fish protein hydrolysates by acid and enzymatic hydrolysis","volume":"4","author":"Wisuthiphaet","year":"2015","journal-title":"J. Med. Bioeng."},{"key":"ref_25","doi-asserted-by":"crossref","first-page":"1328","DOI":"10.1111\/1750-3841.15115","article-title":"Isolation of novel ACE-inhibitory peptide from naked oat globulin hydrolysates in silico approach: Molecular docking, in vivo antihypertension and effects on renin and intracellular endothelin-1","volume":"85","author":"Zheng","year":"2020","journal-title":"J. Food Sci."},{"key":"ref_26","doi-asserted-by":"crossref","first-page":"8161","DOI":"10.1039\/D0FO01240H","article-title":"ACE inhibitory peptides derived from de-fatted lemon basil seeds: Optimization, purification, identification, structure-activity relationship and molecular docking analysis","volume":"11","author":"Kheeree","year":"2020","journal-title":"Food Funct."},{"key":"ref_27","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_28","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_29","doi-asserted-by":"crossref","first-page":"8","DOI":"10.1016\/j.atherosclerosis.2008.06.019","article-title":"Nutritional and nutraceutical approaches to dyslipidemia and atherosclerosis prevention: Focus on dietary proteins","volume":"203","author":"Sirtori","year":"2009","journal-title":"Atherosclerosis"},{"key":"ref_30","doi-asserted-by":"crossref","first-page":"457","DOI":"10.1007\/s00217-017-2968-1","article-title":"Affinity purification of angiotensin-converting enzyme inhibitory peptides from Volutharpa ampullacea perryi protein hydrolysate using Zn-SBA-15 immobilized ACE","volume":"244","author":"Sun","year":"2017","journal-title":"Eur. Food Res. Technol."},{"key":"ref_31","doi-asserted-by":"crossref","first-page":"e13123","DOI":"10.1111\/jfpp.13123","article-title":"Isolation and purification of antioxidant and ACE-inhibitory peptides from Yak (Bos grunniens) skin","volume":"41","author":"Tian","year":"2017","journal-title":"J. Food Process. Preserv."},{"key":"ref_32","doi-asserted-by":"crossref","first-page":"e12275","DOI":"10.1111\/jfbc.12275","article-title":"Purification and identification of Ace-inhibitory peptides from poultry viscera protein hydrolysate","volume":"41","author":"Mane","year":"2017","journal-title":"J. Food Biochem."},{"key":"ref_33","doi-asserted-by":"crossref","first-page":"543","DOI":"10.1016\/j.tifs.2019.04.002","article-title":"Basic and recent advances in marine antihypertensive peptides: Production, structure-activity relationship and bioavailability","volume":"88","author":"Abdelhedi","year":"2019","journal-title":"Trends Food Sci. Technol."},{"key":"ref_34","doi-asserted-by":"crossref","first-page":"121","DOI":"10.1016\/j.foodchem.2011.07.011","article-title":"Studies on purification and the molecular mechanism of a novel ACE inhibitory peptide from whey protein hydrolysate","volume":"130","author":"Pan","year":"2012","journal-title":"Food Chem."},{"key":"ref_35","doi-asserted-by":"crossref","first-page":"438459","DOI":"10.1155\/2014\/438459","article-title":"Angiotensin I converting enzyme inhibitory peptides obtained after in vitro hydrolysis of pea (Pisum sativum var. Bajka) globulins","volume":"2014","author":"Jakubczyk","year":"2014","journal-title":"BioMed Res. Int."},{"key":"ref_36","doi-asserted-by":"crossref","first-page":"3573","DOI":"10.1007\/s00216-018-0925-x","article-title":"Peptidomic strategy for purification and identification of potential ACE-inhibitory and antioxidant peptides in Tetradesmus obliquus microalgae","volume":"410","author":"Montone","year":"2018","journal-title":"Anal. Bioanal. Chem."},{"key":"ref_37","doi-asserted-by":"crossref","first-page":"5230","DOI":"10.1039\/C8FO01146J","article-title":"Isolation, purification and the anti-hypertensive effect of a novel angiotensin I-converting enzyme (ACE) inhibitory peptide from Ruditapes philippinarum fermented with Bacillus natto","volume":"9","author":"Chen","year":"2018","journal-title":"Food Funct."},{"key":"ref_38","doi-asserted-by":"crossref","first-page":"7015","DOI":"10.1021\/acs.jafc.8b01558","article-title":"Isolation and characterization of angiotensin I-converting enzyme (ACE) inhibitory peptides from the enzymatic hydrolysate of carapax trionycis (the shell of the Turtle Pelodiscus sinensis)","volume":"66","author":"Liao","year":"2018","journal-title":"J. Agric. Food Chem."},{"key":"ref_39","doi-asserted-by":"crossref","first-page":"3927","DOI":"10.1007\/s13197-020-04427-0","article-title":"Purification and the secondary structure of a novel angiotensin I-converting enzyme (ACE) inhibitory peptide from the alcalase hydrolysate of seahorse protein","volume":"57","author":"Shi","year":"2020","journal-title":"J. Food Sci. Technol."},{"key":"ref_40","doi-asserted-by":"crossref","first-page":"1961","DOI":"10.1016\/j.procbio.2006.04.019","article-title":"Characterization of an antihypertensive peptide from an Alfalfa white protein hydrolysate produced by a continuous enzymatic membrane reactor","volume":"41","author":"Kapel","year":"2006","journal-title":"Process Biochem."},{"key":"ref_41","doi-asserted-by":"crossref","first-page":"12711","DOI":"10.1039\/D0RA00093K","article-title":"Two novel ACE inhibitory peptides isolated from longan seeds: Purification, inhibitory kinetics and mechanisms","volume":"10","author":"Nuchprapha","year":"2020","journal-title":"RSC Adv."},{"key":"ref_42","doi-asserted-by":"crossref","first-page":"207","DOI":"10.1016\/j.ijbiomac.2017.03.054","article-title":"Enzyme inhibition kinetics and molecular interactions of patatin peptides with angiotensin I-converting enzyme and renin","volume":"101","author":"Fu","year":"2017","journal-title":"Int. J. Biol. Macromol."},{"key":"ref_43","doi-asserted-by":"crossref","first-page":"162","DOI":"10.1002\/jmr.905","article-title":"Studies on molecular recognition between bioactive peptides and angiotensin-converting enzyme","volume":"22","author":"Pina","year":"2009","journal-title":"J. Mol. Recognit."},{"key":"ref_44","doi-asserted-by":"crossref","first-page":"356","DOI":"10.1007\/s10930-013-9492-3","article-title":"Molecular dynamics simulation and molecular docking studies of Angiotensin converting enzyme with inhibitor lisinopril and amyloid beta peptide","volume":"32","author":"Jalkute","year":"2013","journal-title":"Protein J."},{"key":"ref_45","doi-asserted-by":"crossref","first-page":"389","DOI":"10.1016\/j.molliq.2017.11.033","article-title":"Molecular mechanism of interactions between inhibitory tripeptide GEF and angiotensin-converting enzyme in aqueous solutions by molecular dynamic simulations","volume":"249","author":"Qi","year":"2018","journal-title":"J. Mol. Liq."},{"key":"ref_46","doi-asserted-by":"crossref","first-page":"98","DOI":"10.1016\/j.foodchem.2018.02.107","article-title":"Identification of a novel ACE-inhibitory peptide from casein and evaluation of the inhibitory mechanisms","volume":"256","author":"Tu","year":"2018","journal-title":"Food Chem."},{"key":"ref_47","doi-asserted-by":"crossref","first-page":"364","DOI":"10.1039\/C7FO01558E","article-title":"Identification and the molecular mechanism of a novel myosin-derived ACE inhibitory peptide","volume":"9","author":"Yu","year":"2018","journal-title":"Food Funct."},{"key":"ref_48","doi-asserted-by":"crossref","first-page":"211","DOI":"10.1016\/S0169-409X(00)00137-X","article-title":"Delivery systems for penetration enhancement of peptide and protein drugs: Design considerations","volume":"46","author":"Kompella","year":"2001","journal-title":"Adv. Drug Deliv. Rev."},{"key":"ref_49","doi-asserted-by":"crossref","unstructured":"Zheng, Y., Wang, X., Zhuang, Y., Li, Y., Tian, H., Shi, P., and Li, G. (2019). Isolation of novel ACE-inhibitory and antioxidant peptides from quinoa bran albumin assisted with an in silico approach: Characterization, in vivo Antihypertension, and Molecular docking. Molecules, 24.","DOI":"10.3390\/molecules24244562"},{"key":"ref_50","doi-asserted-by":"crossref","unstructured":"Li, J., Liu, Z., Zhao, Y., Zhu, X., Yu, R., Dong, S., and Wu, H. (2018). Novel natural angiotensin converting enzyme (ACE)-inhibitory peptides derived from sea cucumber-modified hydrolysates by adding exogenous proline and a study of their structure(-)activity relationship. Mar. Drugs, 16.","DOI":"10.3390\/md16080271"},{"key":"ref_51","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_52","doi-asserted-by":"crossref","first-page":"e12975","DOI":"10.1111\/jfbc.12975","article-title":"Novel ACE inhibitors derived from soybean proteins using in silico and in vitro studies","volume":"43","author":"Zhao","year":"2019","journal-title":"J. Food Biochem."},{"key":"ref_53","doi-asserted-by":"crossref","first-page":"202","DOI":"10.1080\/07391102.2019.1708798","article-title":"Molecular dynamics simulation and free energy calculation studies of the binding mechanism of allosteric inhibitors with TrkA kinase","volume":"39","author":"Wu","year":"2021","journal-title":"J. Biomol. Struct. Dyn."},{"key":"ref_54","first-page":"1","article-title":"Insight into the binding of ACE-inhibitory peptides to angiotensin-converting enzyme: A molecular simulation","volume":"45","author":"Jiang","year":"2018","journal-title":"Mol. Simul."}],"container-title":["Marine Drugs"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/www.mdpi.com\/1660-3397\/19\/12\/651\/pdf","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2025,10,11]],"date-time":"2025-10-11T07:34:24Z","timestamp":1760168064000},"score":1,"resource":{"primary":{"URL":"https:\/\/www.mdpi.com\/1660-3397\/19\/12\/651"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2021,11,23]]},"references-count":54,"journal-issue":{"issue":"12","published-online":{"date-parts":[[2021,12]]}},"alternative-id":["md19120651"],"URL":"https:\/\/doi.org\/10.3390\/md19120651","relation":{},"ISSN":["1660-3397"],"issn-type":[{"value":"1660-3397","type":"electronic"}],"subject":[],"published":{"date-parts":[[2021,11,23]]}}}