Dynamic combinatorial mass spectrometry leads to metallo-β-lactamase inhibitors
The use of protein ESI mass spectrometry under non-denaturing conditions to analyze a dynamic combinatorial library of thiols/disulfides with the BcII metallo-β-lactamase enabled the rapid identification of an inhibitor with a Ki of 1 μM. The study exemplifies the utility of protein-MS for screening dynamic mixtures of potential enzyme-inhibitors.
Liénard, Beno?t M. R.,Hüting, Rebekka,Lassaux, Patricia,Galleni, Moreno,Frère, Jean-Marie,Schofield, Christopher J.
p. 684 - 688
(2008/09/18)
Cysteinyl peptide inhibitors of Bacillus cereus zinc β-lactamase
Several cysteinyl peptides have been synthesised and shown to be reversible competitive inhibitors of the Bacillus cereus metallo-β-lactamase. The pH dependence of pKi indicates that the thiol anion displaces hydroxide ion from the active site zinc(II). D,D-Peptides bind to the enzyme better than other diastereoisomers, which is compatible with the predicted stereochemistry of the active site.
Bounaga, Sakina,Galleni, Moreno,Laws, Andrew P,Page, Michael I
p. 503 - 510
(2007/10/03)
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