A novel competitive class of alpha-glucosidase inhibitors: (E)-1-phenyl-3-(4-styrylphenyl)urea derivatives = 신규한 알파 글루코시다아제 경쟁적 저해제: (E)-1-Phenyl-3-(4-styrylphenyl)urea 유도체

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dc.contributor.authorJ Y Kim-
dc.contributor.authorJ W Lee-
dc.contributor.authorY S Kim-
dc.contributor.authorY Lee-
dc.contributor.authorYoung Bae Ryu-
dc.contributor.authorS Kim-
dc.contributor.authorHyung Won Ryu-
dc.contributor.authorM J Curtis-Long-
dc.contributor.authorK W Lee-
dc.contributor.authorWoo Song Lee-
dc.contributor.authorK H Park-
dc.date.accessioned2017-04-19T09:19:53Z-
dc.date.available2017-04-19T09:19:53Z-
dc.date.issued2010-
dc.identifier.issn1439-4227-
dc.identifier.uri10.1002/cbic.201000376.ko
dc.identifier.urihttps://oak.kribb.re.kr/handle/201005/9778-
dc.description.abstractCompetitive glycosidase inhibitors are generally sugar mimics that are costly and tedious to obtain because they require challenging and elongated chemical synthesis, which must be stereo- and regiocontrolled. Here, we show that readily accessible achiral (E)-1-phenyl-3-(4-strylphenyl)ureas are potent competitive α-glucosidase inhibitors. A systematic synthesis study shows that the 1-phenyl moiety on the urea is critical for ensuring competitive inhibition, and substituents on both terminal phenyl groups contribute to inhibition potency. The most potent inhibitor, compound 12 (IC(50)=8.4 μM, K(i)=3.2 μM), manifested a simple slow-binding inhibition profile for α-glucosidase with the kinetic parameters k(3)=0.005256 μM(-1)?min(-1), k(4)=0.003024 min(-1), and K(i)(app) =0.5753 μM.-
dc.publisherWiley-
dc.titleA novel competitive class of alpha-glucosidase inhibitors: (E)-1-phenyl-3-(4-styrylphenyl)urea derivatives = 신규한 알파 글루코시다아제 경쟁적 저해제: (E)-1-Phenyl-3-(4-styrylphenyl)urea 유도체-
dc.title.alternativeA novel competitive class of alpha-glucosidase inhibitors: (E)-1-phenyl-3-(4-styrylphenyl)urea derivatives-
dc.typeArticle-
dc.citation.titleChembiochem-
dc.citation.number15-
dc.citation.endPage2131-
dc.citation.startPage2125-
dc.citation.volume11-
dc.contributor.affiliatedAuthorYoung Bae Ryu-
dc.contributor.affiliatedAuthorHyung Won Ryu-
dc.contributor.affiliatedAuthorWoo Song Lee-
dc.contributor.alternativeName김준영-
dc.contributor.alternativeName이지원-
dc.contributor.alternativeName김영수-
dc.contributor.alternativeName이유노-
dc.contributor.alternativeName류영배-
dc.contributor.alternativeName김송미-
dc.contributor.alternativeName류형원-
dc.contributor.alternativeNameCurtis-Long-
dc.contributor.alternativeName이근우-
dc.contributor.alternativeName이우송-
dc.contributor.alternativeName박기훈-
dc.identifier.bibliographicCitationChembiochem, vol. 11, no. 15, pp. 2125-2131-
dc.identifier.doi10.1002/cbic.201000376-
dc.subject.keywordalpha-glucosidases-
dc.subject.keyworddrug design-
dc.subject.keywordinhibitors-
dc.subject.keywordstructureactivity relationships-
dc.subject.keywordurea stilbene-
dc.subject.localα-glucosidase-
dc.subject.localα-Glucosidase-
dc.subject.localAlpha-glucosidase-
dc.subject.localalpha-glucosidases-
dc.subject.localdrug design-
dc.subject.localDrug design-
dc.subject.localinhibitors-
dc.subject.localInhibitors-
dc.subject.localinhibitor-
dc.subject.localInhibitor-
dc.subject.localstructure-activity relationships-
dc.subject.localStructure-activity relationship-
dc.subject.localstructureactivity relationships-
dc.subject.localStructure-activity relationships-
dc.subject.localstructure-activity relationship-
dc.subject.localurea stilbene-
dc.description.journalClassY-
Appears in Collections:
Jeonbuk Branch Institute > Functional Biomaterial Research Center > 1. Journal Articles
Ochang Branch Institute > Natural Product Research Center > 1. Journal Articles
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