Article ID | Journal | Published Year | Pages | File Type |
---|---|---|---|---|
1367384 | Bioorganic & Medicinal Chemistry Letters | 2006 | 7 Pages |
Abstract
Homo-cysteinyl peptides were found to be more active than cysteinyl peptides toward L1 metallo-β-lactamase as reversible competitive inhibitors. A combinatorial library of more than 90 homo-cysteinyl peptides was synthesized and screened for their inhibitory activity toward the L1 enzyme. A systematic structure–activity relationship analysis has revealed the preferred interaction groups for L1 conserved binding sites of β-lactam substrates. The most active compound 95b, had a Ki of 2.1 nM.
Graphical abstractHomo-cysteinyl peptides library was synthesized and screened for their inhibitory activity toward L1 metallo-β-lactamase. The most active compound had a Ki of 2.1 nM.Figure optionsDownload full-size imageDownload as PowerPoint slide
Related Topics
Physical Sciences and Engineering
Chemistry
Organic Chemistry
Authors
Qin Sun, Andy Law, Michael W. Crowder, H. Mario Geysen,