Article ID Journal Published Year Pages File Type
1367384 Bioorganic & Medicinal Chemistry Letters 2006 7 Pages PDF
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
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