Structural Evidence for Antihypertensive Effect of an Antioxidant Peptide Purified from the Edible Marine Animal Styela clava SCIE SCOPUS KCI

DC Field Value Language
dc.contributor.author Kang, Nalae -
dc.contributor.author Ko, Seok-Chun -
dc.contributor.author Kim, Hyun-Soo -
dc.contributor.author Yang, Hye-Won -
dc.contributor.author Ahn, Ginnae -
dc.contributor.author Lee, Seung-Cheol -
dc.contributor.author Lee, Tae-Gee -
dc.contributor.author Lee, Jung-Suck -
dc.contributor.author Jeon, You-Jin -
dc.date.accessioned 2020-12-10T07:55:04Z -
dc.date.available 2020-12-10T07:55:04Z -
dc.date.created 2020-05-27 -
dc.date.issued 2020-02 -
dc.identifier.issn 1096-620X -
dc.identifier.uri https://sciwatch.kiost.ac.kr/handle/2020.kiost/38741 -
dc.description.abstract This study investigated the antihypertensive effects of an antioxidant peptide, Leu-Trp-His-Thr-His (LWHTH), purified from Styela clava peptic hydrolysate, to assess the bioactivity of the peptide and verify the value of S. clava as a health-promoting food. Also, the study presented structural evidence for the effects of LWHTH. The inhibitory effect of LWHTH on angiotensin I-converting enzyme (ACE) was assessed using enzyme reaction methods and the simulation methods in computational space. LWHTH inhibited ACE with an IC50 value of 16.42 +/- 0.45 mu M. The LWHTH structure was stable, and its ACE inhibitory effect was retained under simulated gastrointestinal conditions. In silico simulations revealed that LWHTH binds the active site of ACE, with residues LW making the ACE-LWHTH complex stable and residues HTH making the complex strong. Furthermore, LWHTH significantly reduced blood pressure in spontaneously hypertensive rats. These results demonstrate that LWHTH has the potential to be a healthy functional food with antihypertensive effects. Therefore, S. clava consumption may be beneficial for human health. -
dc.description.uri 1 -
dc.language English -
dc.publisher MARY ANN LIEBERT, INC -
dc.title Structural Evidence for Antihypertensive Effect of an Antioxidant Peptide Purified from the Edible Marine Animal Styela clava -
dc.type Article -
dc.citation.endPage 138 -
dc.citation.startPage 132 -
dc.citation.title JOURNAL OF MEDICINAL FOOD -
dc.citation.volume 23 -
dc.citation.number 2 -
dc.contributor.alternativeName 강나래 -
dc.identifier.bibliographicCitation JOURNAL OF MEDICINAL FOOD, v.23, no.2, pp.132 - 138 -
dc.identifier.doi 10.1089/jmf.2019.4415 -
dc.identifier.scopusid 2-s2.0-85078977610 -
dc.identifier.wosid 000510807000004 -
dc.type.docType Article -
dc.identifier.kciid ART002558791 -
dc.description.journalClass 1 -
dc.description.isOpenAccess N -
dc.subject.keywordPlus ACE INHIBITORY PEPTIDE -
dc.subject.keywordPlus CONVERTING-ENZYME ACE -
dc.subject.keywordPlus BIOACTIVE PEPTIDES -
dc.subject.keywordPlus MOLECULAR DOCKING -
dc.subject.keywordPlus SKIN -
dc.subject.keywordPlus PURIFICATION -
dc.subject.keywordPlus KINETICS -
dc.subject.keywordAuthor angiotensin I-converting enzyme -
dc.subject.keywordAuthor antioxidant peptide -
dc.subject.keywordAuthor blood pressure -
dc.subject.keywordAuthor molecular docking -
dc.subject.keywordAuthor Styela clava -
dc.relation.journalWebOfScienceCategory Chemistry, Medicinal -
dc.relation.journalWebOfScienceCategory Food Science & Technology -
dc.relation.journalWebOfScienceCategory Nutrition & Dietetics -
dc.description.journalRegisteredClass scie -
dc.description.journalRegisteredClass scopus -
dc.description.journalRegisteredClass kci -
dc.relation.journalResearchArea Pharmacology & Pharmacy -
dc.relation.journalResearchArea Food Science & Technology -
dc.relation.journalResearchArea Nutrition & Dietetics -
Appears in Collections:
Jeju Research Institute > Jeju Bio Research Center > 1. Journal Articles
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