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Bioorg Med Chem Lett. 2006 Oct 1;16(19):5169-75. Epub 2006 Jul 27.

Homo-cysteinyl peptide inhibitors of the L1 metallo-beta-lactamase, and SAR as determined by combinatorial library synthesis.

Author information

1
Department of Chemistry, University of Virginia, McCormick Road, PO Box 400319, Charlottesville, 22904, USA.

Abstract

Homo-cysteinyl peptides were found to be more active than cysteinyl peptides toward L1 metallo-beta-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 beta-lactam substrates. The most active compound 95b, had a K(i) of 2.1 nM.

PMID:
16875814
DOI:
10.1016/j.bmcl.2006.07.001
[Indexed for MEDLINE]

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