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

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dc.contributor.authorKang, Nalae-
dc.contributor.authorKo, Seok-Chun-
dc.contributor.authorKim, Hyun-Soo-
dc.contributor.authorYang, Hye-Won-
dc.contributor.authorAhn, Ginnae-
dc.contributor.authorLee, Seung-Cheol-
dc.contributor.authorLee, Tae-Gee-
dc.contributor.authorLee, Jung-Suck-
dc.contributor.authorJeon, You-Jin-
dc.date.accessioned2022-12-26T13:02:43Z-
dc.date.available2022-12-26T13:02:43Z-
dc.date.issued2020-02-
dc.identifier.issn1096-620X-
dc.identifier.issn1557-7600-
dc.identifier.urihttps://scholarworks.gnu.ac.kr/handle/sw.gnu/6938-
dc.description.abstractThis 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.format.extent7-
dc.language영어-
dc.language.isoENG-
dc.publisher한국식품영양과학회-
dc.titleStructural Evidence for Antihypertensive Effect of an Antioxidant Peptide Purified from the Edible Marine Animal Styela clava-
dc.typeArticle-
dc.publisher.location대한민국-
dc.identifier.doi10.1089/jmf.2019.4415-
dc.identifier.scopusid2-s2.0-85078977610-
dc.identifier.wosid000510807000004-
dc.identifier.bibliographicCitationJournal of Medicinal Food, v.23, no.2, pp 132 - 138-
dc.citation.titleJournal of Medicinal Food-
dc.citation.volume23-
dc.citation.number2-
dc.citation.startPage132-
dc.citation.endPage138-
dc.type.docTypeArticle-
dc.identifier.kciidART002558791-
dc.description.isOpenAccessN-
dc.description.journalRegisteredClassscie-
dc.description.journalRegisteredClassscopus-
dc.description.journalRegisteredClasskci-
dc.relation.journalResearchAreaPharmacology & Pharmacy-
dc.relation.journalResearchAreaFood Science & Technology-
dc.relation.journalResearchAreaNutrition & Dietetics-
dc.relation.journalWebOfScienceCategoryChemistry, Medicinal-
dc.relation.journalWebOfScienceCategoryFood Science & Technology-
dc.relation.journalWebOfScienceCategoryNutrition & Dietetics-
dc.subject.keywordPlusACE INHIBITORY PEPTIDE-
dc.subject.keywordPlusCONVERTING-ENZYME ACE-
dc.subject.keywordPlusBIOACTIVE PEPTIDES-
dc.subject.keywordPlusMOLECULAR DOCKING-
dc.subject.keywordPlusSKIN-
dc.subject.keywordPlusPURIFICATION-
dc.subject.keywordPlusKINETICS-
dc.subject.keywordAuthorangiotensin I-converting enzyme-
dc.subject.keywordAuthorantioxidant peptide-
dc.subject.keywordAuthorblood pressure-
dc.subject.keywordAuthormolecular docking-
dc.subject.keywordAuthorStyela clava-
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