Abstract
A small set of boronic acids acting as low nanomolar inhibitors of AmpC beta-lactamase were designed and synthesized in the effort to improve affinity, pharmacokinetic properties, and to provide a valid lead compound. X-ray crystallography revealed the binary complex of the best inhibitor bound to the enzyme, highlighting possibilities for its further rational derivatization and chemical optimization.
Copyright 2010 Elsevier Ltd. All rights reserved.
Publication types
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Research Support, N.I.H., Extramural
MeSH terms
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Bacterial Proteins / antagonists & inhibitors*
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Boronic Acids / chemistry
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Boronic Acids / pharmacology*
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Enzyme Inhibitors / chemistry
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Enzyme Inhibitors / pharmacology*
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Models, Molecular
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Protein Conformation
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beta-Lactamase Inhibitors*
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beta-Lactamases
Substances
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Bacterial Proteins
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Boronic Acids
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Enzyme Inhibitors
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beta-Lactamase Inhibitors
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AmpC beta-lactamases
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beta-Lactamases
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benzeneboronic acid