Inhibition kinetics, molecular docking, and stability studies of the effect of papain-generated peptides from palm kernel cake proteins on angiotensin-converting enzyme (ACE)

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dc.contributor.authorZarei, Mohammaden
dc.contributor.authorGhanbari, Rahelehen
dc.contributor.authorZainal, Najiben
dc.contributor.authorOvissipour, Rezaen
dc.contributor.authorSaari, Nazamiden
dc.date.accessioned2023-01-10T14:04:41Zen
dc.date.available2023-01-10T14:04:41Zen
dc.date.issued2022-12-30en
dc.date.updated2023-01-09T20:47:24Zen
dc.description.abstractThree novel peptide sequences YGIKVGYAIP, GGIF, and GIFE from papain-generated protein hydrolysate of palm kernel cake proteins were used for stability study against ACE, ACE-inhibition kinetics, and molecular docking studies. Results showed that peptide YGIKVGYAIP was degraded, and its ACE-inhibitory activity decreased after 3 h pre-incubation with ACE, while peptides GGIF and GIFE were resistant. However, although the ACE-inhibitory activity of GIFE increased during this time, the ACE inhibitory activity of GGIF decreased after pre-incubation with ACE, indicating that peptide. YGIKVGYAIP and GGIF are substrate-type, whereas GIFE is a true-inhibitor type. Peptide YGIKVGYAIP showed the lowest Ki (0.054 mM) in the inhibition kinetics study compared to GGIF and GIFE, with Ki of 1.27 m M and 18 mM, respectively. In addition, YGIKVGYAIP revealed the lowest Km and Vmax and higher CE in different peptide concentrations, implying that the enzyme catalysis decreased, and peptides had some binding affinity to the enzyme in lower concentrations, which led to reduced catalytic ability. Furthermore, YGIKVGYAIP showed the lowest docking score of −14.733 and 21 interactions with tACE, while GGIF revealed the higher docking score of −8.006 with 15 interactions with tACE.en
dc.description.versionPublished versionen
dc.format.mimetypeapplication/pdfen
dc.identifier100147 (Article number)en
dc.identifier.doihttps://doi.org/10.1016/j.fochms.2022.100147en
dc.identifier.eissn2666-5662en
dc.identifier.issn2666-5662en
dc.identifier.orcidOvissipour, Reza [0000-0002-5564-0094]en
dc.identifier.orcidZarei, Mohammad [0000-0003-1573-347X]en
dc.identifier.otherPMC9789325en
dc.identifier.otherS2666-5662(22)00075-2 (PII)en
dc.identifier.pmid36573107en
dc.identifier.urihttp://hdl.handle.net/10919/113109en
dc.identifier.volume5en
dc.language.isoenen
dc.publisherElsevieren
dc.relation.urihttps://www.ncbi.nlm.nih.gov/pubmed/36573107en
dc.rightsCreative Commons Attribution 4.0 Internationalen
dc.rights.urihttp://creativecommons.org/licenses/by/4.0/en
dc.subjectAngiotensin-converting enzyme inhibitory peptideen
dc.subjectKineticsen
dc.subjectMolecular dockingen
dc.subjectPalm kernel cakeen
dc.subject5.1 Pharmaceuticalsen
dc.subject5 Development of treatments and therapeutic interventionsen
dc.titleInhibition kinetics, molecular docking, and stability studies of the effect of papain-generated peptides from palm kernel cake proteins on angiotensin-converting enzyme (ACE)en
dc.title.serialFood Chemistry: Molecular Sciencesen
dc.typeArticle - Refereeden
dc.type.dcmitypeTexten
dc.type.otherJournal Articleen
dcterms.dateAccepted2022-11-12en
pubs.organisational-group/Virginia Techen
pubs.organisational-group/Virginia Tech/Agriculture & Life Sciencesen
pubs.organisational-group/Virginia Tech/Agriculture & Life Sciences/Virginia Seafood ARECen
pubs.organisational-group/Virginia Tech/All T&R Facultyen
pubs.organisational-group/Virginia Tech/Agriculture & Life Sciences/CALS T&R Facultyen

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