Show simple item record

dc.contributor.authorDong, Jing( China Pharmaceut Univ, Sch Life Sci & Technol)
dc.contributor.authorYu, Heguo(Shanghai Inst Planned Parenthood Res)
dc.contributor.authorZhang, Yonglian(Shanghai Inst Planned Parenthood Res)
dc.contributor.authorDiao, Hua(Shanghai Inst Planned Parenthood Res)
dc.contributor.authorLin, Donghai
dc.contributor.author林东海
dc.date.accessioned2012-02-19T04:04:54Z
dc.date.available2012-02-19T04:04:54Z
dc.date.issued2011
dc.identifier.citationPROTEIN AND PEPTIDE LETTERS,2011,18(11):1126-1132zh_CN
dc.identifier.issn0929-8665
dc.identifier.uriWOS:000298538600009
dc.identifier.urihttps://dspace.xmu.edu.cn/handle/2288/11464
dc.description.abstractHuman beta-defensin 3 (DEFB103) is a recently identified small cysteine-rich cationic peptide expressed ubiquitously upon local microbial invasion. A number of accumulating evidences indicate that this peptide is involved in many biological processes, including microbicidal activities, chemoattraction, and immunomodulation. In this article, we describe a novel approach through which we performed the expression and purification of the recombinant DEFB103 peptide in Escherichia coli (E. coli) based on the pTWIN1 expression system. This approach does not introduce any extra residues to the peptide product, and also eliminates the requirement of removing the fusion tag by exogenous proteases. A high yield of 112 mg of soluble fusion DEFB103 was obtained in 1 liter of Luria-Bertani (LB) medium. By one-step affinity chromatography and on-column, auto-cleavage of the fusion tag, the mature DEFB103 peptide was produced with a yield of 30 mg/L LB. The purified DEFB103 peptide demonstrated strong antimicrobial activities against E. coli, S. aureus and C. albicans, which were representatives of Gram-negative and Gram-positive bacteria and fungi, respectively. Using this novel approach, we have successfully expressed and purified several human defensins with significant bioactivities. Our work may be helpful for structural and functional studies of other human defensins, and also for the production of human defensins.zh_CN
dc.description.sponsorshipProgram of Shanghai Subject Chief Scientist[09XD1405100]zh_CN
dc.language.isoenzh_CN
dc.publisherBENTHAM SCIENCE PUBL LTDzh_CN
dc.subjectExpressionzh_CN
dc.subjectpurificationzh_CN
dc.subjectinteinzh_CN
dc.subjecthuman beta-defensin3zh_CN
dc.subjectantimicrobial activityzh_CN
dc.titleSoluble Fusion Expression and Characterization of Human Beta-defensin 3 Using a Novel Approachzh_CN
dc.typeArticlezh_CN


Files in this item

Thumbnail

This item appears in the following Collection(s)

Show simple item record