The influence of flavonoid compounds on the in vitro inhibition study of a human fibroblast collagenase catalytic domain expressed in E. coli

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dc.contributor.authorT T H Nguyen-
dc.contributor.authorY H Moon-
dc.contributor.authorYoung Bae Ryu-
dc.contributor.authorYoung Min Kim-
dc.contributor.authorS H Nam-
dc.contributor.authorM S Kim-
dc.contributor.authorA Kimura-
dc.contributor.authorD Kim-
dc.date.accessioned2017-04-19T09:35:49Z-
dc.date.available2017-04-19T09:35:49Z-
dc.date.issued2013-
dc.identifier.issn0141-0229-
dc.identifier.uri10.1016/j.enzmictec.2012.10.001ko
dc.identifier.urihttps://oak.kribb.re.kr/handle/201005/11081-
dc.description.abstractThe human fibroblast collagenase catalytic domain (MMP1ca) that is considered a prototype for all interstitial collagenase and plays an important role in the turnover of collagen fibrils in the matrix was expressed as an inclusion body in the Escherichia coli. The purified enzyme displayed activity with substrate Dnp-Pro-Leu-Ala-Leu-Trp-Ala-Arg-OH with a Km value of 26.61±1.42μM. The inhibition activity of the nine flavonoid compounds and gallic acid against MMP1ca was examined. Among the compounds tested, the IC50 of seven flavonoid compoundswere determined and ranged from 14.13 to 339.21μM. Epigallocatechin gallate (EGCG) showed the highest inhibition toward MMP1ca with IC50 values of 14.13±0.49μM. EGCG showed a competitive inhibition pattern with a Ki value of 10.47±0.51μM. The free binding energy of EGCG against MMP1ca was -13.07kcalmol-1, which was calculated by using Autodock 3.0.5 software and showed numerous hydrophobic and hydrogen bond interactions. Thegalloyl group of EGCG, gallocatechin gallate and epicatechin gallate was determined to be important for inhibitory activity against MMP1ca.-
dc.publisherElsevier-
dc.titleThe influence of flavonoid compounds on the in vitro inhibition study of a human fibroblast collagenase catalytic domain expressed in E. coli-
dc.title.alternativeThe influence of flavonoid compounds on the in vitro inhibition study of a human fibroblast collagenase catalytic domain expressed in E. coli-
dc.typeArticle-
dc.citation.titleEnzyme and Microbial Technology-
dc.citation.number1-
dc.citation.endPage31-
dc.citation.startPage26-
dc.citation.volume52-
dc.contributor.affiliatedAuthorYoung Bae Ryu-
dc.contributor.affiliatedAuthorYoung Min Kim-
dc.contributor.alternativeNameNguyen-
dc.contributor.alternativeName문영환-
dc.contributor.alternativeName류영배-
dc.contributor.alternativeName김영민-
dc.contributor.alternativeName남승희-
dc.contributor.alternativeName김미숙-
dc.contributor.alternativeNameKimura-
dc.contributor.alternativeName김도만-
dc.identifier.bibliographicCitationEnzyme and Microbial Technology, vol. 52, no. 1, pp. 26-31-
dc.identifier.doi10.1016/j.enzmictec.2012.10.001-
dc.subject.keywordCatechin-
dc.subject.keywordEpigallocatechin gallate-
dc.subject.keywordExpression-
dc.subject.keywordInhibition-
dc.subject.keywordMatrix metalloproteinase MMP-1-
dc.subject.keywordMolecular docking-
dc.subject.localCatechin-
dc.subject.localcatechin-
dc.subject.localEpigallocatechin gallate-
dc.subject.localexpression-
dc.subject.localExpression-
dc.subject.localinhibition-
dc.subject.localInhibition-
dc.subject.localMatrix metalloproteinase MMP-1-
dc.subject.localMatrix metalloproteinase-1-
dc.subject.localmatrix metalloproteinase (MMP)-1-
dc.subject.localmatrix metalloproteinase-1-
dc.subject.localmatrix metalloproteinase-1 inhibitor-
dc.subject.localmolecular docking-
dc.subject.localMolecular docking-
dc.description.journalClassY-
Appears in Collections:
Jeonbuk Branch Institute > Functional Biomaterial Research Center > 1. Journal Articles
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