Unique binding mode of Evogliptin with human dipeptidyl peptidase IV

Cited 3 time in webofscience Cited 0 time in scopus
  • Hit : 232
  • Download : 0
DC FieldValueLanguage
dc.contributor.authorLee, Hyung Kiko
dc.contributor.authorKim, Mi-Kyungko
dc.contributor.authorKim, Ha Dongko
dc.contributor.authorKim, Heung Jaeko
dc.contributor.authorKim, Ji Wonko
dc.contributor.authorLee, Jie-Ohko
dc.contributor.authorKim, Chan-Whako
dc.contributor.authorKim, Eunice EunKyeongko
dc.date.accessioned2018-01-22T02:04:08Z-
dc.date.available2018-01-22T02:04:08Z-
dc.date.created2017-12-18-
dc.date.created2017-12-18-
dc.date.issued2017-12-
dc.identifier.citationBIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS, v.494, no.3-4, pp.452 - 459-
dc.identifier.issn0006-291X-
dc.identifier.urihttp://hdl.handle.net/10203/237153-
dc.description.abstractEvogliptin ((R)-4-((R)-3-amino-4-(2,4,5-trifluorophenyl)butanoyl)-3-(tert-butoxymethyl)piperazine-2-one)) is a highly potent selective inhibitor of dipeptidyl peptidase IV (DPP4) that was approved for the treatment of type 2 diabetes in South Korea. In this study, we report the crystal structures of Evogliptin, DA-12166, and DA-12228 (S,R diastereomer of Evogliptin) complexed to human DPP4. Analysis of both the structures and inhibitory activities suggests that the binding of the trifluorophenyl moiety in the S-1 pocket and the piperazine-2-one moiety have hydrophobic interactions with Phe357 in the S-2 extensive subsite, and that the multiple hydrogen bonds made by the (R)-beta-amine group in the S-2 pocket and the contacts made by the (R)-tert-butyl group with Arg125 contribute to the high potency observed for Evogliptin. (c) 2017 Elsevier Inc. All rights reserved.-
dc.languageEnglish-
dc.publisherACADEMIC PRESS INC ELSEVIER SCIENCE-
dc.subjectHIGHLY POTENT-
dc.subjectPRECLINICAL PROFILE-
dc.subjectINHIBITOR-
dc.subjectDISCOVERY-
dc.subjectSYSTEM-
dc.titleUnique binding mode of Evogliptin with human dipeptidyl peptidase IV-
dc.typeArticle-
dc.identifier.wosid000416393300005-
dc.identifier.scopusid2-s2.0-85032980700-
dc.type.rimsART-
dc.citation.volume494-
dc.citation.issue3-4-
dc.citation.beginningpage452-
dc.citation.endingpage459-
dc.citation.publicationnameBIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS-
dc.identifier.doi10.1016/j.bbrc.2017.10.101-
dc.contributor.localauthorLee, Jie-Oh-
dc.contributor.nonIdAuthorLee, Hyung Ki-
dc.contributor.nonIdAuthorKim, Mi-Kyung-
dc.contributor.nonIdAuthorKim, Ha Dong-
dc.contributor.nonIdAuthorKim, Heung Jae-
dc.contributor.nonIdAuthorKim, Chan-Wha-
dc.contributor.nonIdAuthorKim, Eunice EunKyeong-
dc.description.isOpenAccessN-
dc.type.journalArticleArticle-
dc.subject.keywordAuthorDipeptidyl peptidase IV-
dc.subject.keywordAuthorDPP4-
dc.subject.keywordAuthorEvogliptin-
dc.subject.keywordAuthorDiabetes-
dc.subject.keywordAuthorInhibitor-
dc.subject.keywordAuthorComplex structure-
dc.subject.keywordPlusHIGHLY POTENT-
dc.subject.keywordPlusPRECLINICAL PROFILE-
dc.subject.keywordPlusINHIBITOR-
dc.subject.keywordPlusDISCOVERY-
dc.subject.keywordPlusSYSTEM-
Appears in Collection
CH-Journal Papers(저널논문)
Files in This Item
There are no files associated with this item.
This item is cited by other documents in WoS
⊙ Detail Information in WoSⓡ Click to see webofscience_button
⊙ Cited 3 items in WoS Click to see citing articles in records_button

qr_code

  • mendeley

    citeulike


rss_1.0 rss_2.0 atom_1.0