Recombinant expression, antimicrobial activity and mechanism of action of tritrpticin analogs containing fluoro-tryptophan residues
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- 作者：Mauricio Ariasa ; Elesha R. Hoffartha ; 1 ; Hiroaki Ishidaa ; James M. Araminib ; Hans J. Vogela ; vogel@ucalgary.ca" class="auth_mail" title="E-mail the corresponding author
- 关键词：AMPs ; antimicrobial peptides ; ePC ; egg-derived l-α-phosphatidylcholine ; ePG ; egg-derived l-α-phosphatidylglycerol ; IPTG ; isopropyl β-d-thiogalactopyranoside ; LUVs ; large unilamellar vesicles ; MIC ; minimal inhibitory concentration ; MBC ; minimal bactericidal concentration ; NMR ; nuclear magnetic resonance ; NCF ; nitrocefin ; ONPG ; 2-nitrophenyl-β-d-galactopyranoside ; SDS ; sodium dodecyl sulfate ; TEV ; tobacco etch virus
- 刊名：Biochimica et Biophysica Acta (BBA)-Biomembranes
- 出版年：2016
- 出版时间：May 2016
- 年：2016
- 卷：1858
- 期：5
- 页码：1012-1023
- 全文大小：1917 K
文摘
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Introduction of unnatural amino acids may improve the activity of AMPs.
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Fluorinated analogs of tritrpticin were created by insertion of fluoro-tryptophans.
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These analogs preserved the killing activity and mechanism of action of tritrpticin.
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19F NMR could differentiate the contributions of individual Trp in a membrane model.