{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,1,1]],"date-time":"2026-01-01T09:46:36Z","timestamp":1767260796874,"version":"3.37.3"},"reference-count":41,"publisher":"Wiley","license":[{"start":{"date-parts":[[2018,1,1]],"date-time":"2018-01-01T00:00:00Z","timestamp":1514764800000},"content-version":"unspecified","delay-in-days":0,"URL":"http:\/\/creativecommons.org\/licenses\/by\/4.0\/"}],"funder":[{"name":"Science and Technology Research and Development Plan of Weihai","award":["2010-3-96","WH2016","HIT.NSRIF.201709"],"award-info":[{"award-number":["2010-3-96","WH2016","HIT.NSRIF.201709"]}]},{"DOI":"10.13039\/501100003472","name":"Harbin Institute of Technology","doi-asserted-by":"publisher","award":["2010-3-96","WH2016","HIT.NSRIF.201709"],"award-info":[{"award-number":["2010-3-96","WH2016","HIT.NSRIF.201709"]}],"id":[{"id":"10.13039\/501100003472","id-type":"DOI","asserted-by":"publisher"}]},{"name":"Research Fund of the Central Universities","award":["2010-3-96","WH2016","HIT.NSRIF.201709"],"award-info":[{"award-number":["2010-3-96","WH2016","HIT.NSRIF.201709"]}]}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["BioMed Research International"],"published-print":{"date-parts":[[2018]]},"abstract":"<jats:p>ACE inhibitory dipeptides from<jats:italic> Xerocomus badius<\/jats:italic> fermented shrimp processing waste were isolated with ethanol, macroporous resin, chloroform, and Sephadex G-10 in sequence and identified by LC-MS\/MS system coupled with electrospray ionization source. Molecular docking was performed for exploring the mechanism of their inhibitions. The results showed that the identified ACE inhibitory dipeptides were Cys-Cys and Cys-Arg with IC<jats:sub>50<\/jats:sub> values of 4.37 \u00b1 0.07 and 475.95 \u00b1 0.11\u2009<jats:italic>\u03bc<\/jats:italic>M, respectively. The difference between ACE inhibitor potency of Cys-Cys and Cys-Arg could be explained by results of molecular docking. Cys-Cys formed crucial coordination between carboxyl oxygen and Zn(II), hydrogen bonds with residues Ala354(O), Ala356(HN), and Tyr523(OH), and a bump with the residue His387(NE2) at the active site of ACE. There was no coordination, except for 5 hydrogen bonds (at residues His353, Ala354, Glu384, Glu403, and Arg522) and a bump (Glu411) between Cys-Arg and active site of ACE. These findings highlighted that Cys-Cys could be considered as a novel potent ACE inhibitor, and coordination between its carboxyl oxygen and Zn(II) played significant role in defining its ACE inhibitor potency.<\/jats:p>","DOI":"10.1155\/2018\/5089270","type":"journal-article","created":{"date-parts":[[2018,5,8]],"date-time":"2018-05-08T19:32:12Z","timestamp":1525807932000},"page":"1-9","source":"Crossref","is-referenced-by-count":9,"title":["Identification and Functional Mechanism of Novel Angiotensin I Converting Enzyme Inhibitory Dipeptides from<i> Xerocomus badius<\/i> Cultured in Shrimp Processing Waste Medium"],"prefix":"10.1155","volume":"2018","author":[{"ORCID":"https:\/\/orcid.org\/0000-0002-5008-4789","authenticated-orcid":true,"given":"Xiujun","family":"Gao","sequence":"first","affiliation":[{"name":"School of Marine Science and Technology, Harbin Institute of Technology, Weihai, West Culture Road 2, Weihai, Shandong 264209, 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