Article ID | Journal | Published Year | Pages | File Type |
---|---|---|---|---|
10587269 | Bioorganic & Medicinal Chemistry Letters | 2013 | 33 Pages |
Abstract
In an effort to test whether a transition state analog is an inhibitor of the metallo-β-lactamases, a phospholactam analog of carbapenem has been synthesized and characterized. The phospholactam 1 proved to be a weak, time-dependent inhibitor of IMP-1 (70%), CcrA (70%), L1 (70%), NDM-1 (53%), and Bla2 (94%) at an inhibitor concentration of 100 μM. The phospholactam 1 activated ImiS and BcII at the same concentration. Docking studies were used to explain binding and to offer suggestions for modifications to the phospholactam scaffold to improve binding affinities.
Keywords
Related Topics
Physical Sciences and Engineering
Chemistry
Organic Chemistry
Authors
Ke-Wu Yang, Lei Feng, Shao-Kang Yang, Mahesh Aitha, Alecander E. LaCuran, Peter Oelschlaeger, Michael W. Crowder,