Structure Guided Development of Potent Reversibly Binding Penicillin Binding Protein Inhibitors
ACS Medicinal Chemistry Letters2011Vol. 2(3), pp. 219–223
Citations Over TimeTop 19% of 2011 papers
Esther C. Y. Woon, Astrid Zervosen, E. Sauvage, Katie J. Simmons, Matej Živec, Steven R. Inglis, Colin W. G. Fishwick, Stanislav Gobec, P. Charlier, André Luxen, Christopher J. Schofield
Abstract
Following from the evaluation of different types of electrophiles, combined modeling and crystallographic analyses are used to generate potent boronic acid based inhibitors of a penicillin binding protein. The results suggest that a structurally informed approach to penicillin binding protein inhibition will be useful for the development of both improved reversibly binding inhibitors, including boronic acids, and acylating inhibitors, such as β-lactams.
Related Papers
- → Variation in penicillin-binding protein patterns of penicillin-resistant clinical isolates of pneumococci(1989)95 cited
- → 4.07 Electrophilic Cyclization(2014)16 cited
- → Alterations in kinetic properties of penicillin-binding proteins of penicillin-resistant Streptococcus pneumoniae(1986)42 cited
- → Some reactions of soft electrophiles with esters and other compounds containing the thiocarbonyl group(1976)18 cited
- → Isomeric exocyclic and endocyclic dienolates: behavior towards electrophiles(1985)7 cited