Your browser doesn't support javascript.
loading
Show: 20 | 50 | 100
Results 1 - 1 de 1
Filter
Add more filters










Database
Language
Publication year range
1.
J Chem Inf Model ; 54(2): 362-6, 2014 Feb 24.
Article in English | MEDLINE | ID: mdl-24444037

ABSTRACT

Small molecules used in fragment-based drug discovery form multiple, promiscuous binding complexes difficult to capture experimentally. Here, we identify such binding poses and their associated energetics and kinetics using molecular dynamics simulations on AmpC ß-lactamase. Only one of the crystallographic binding poses was found to be thermodynamically favorable; however, the ligand shows several binding poses within the pocket. This study demonstrates free-binding molecular simulations in the context of fragment-to-lead development and its potential application in drug design.


Subject(s)
Bacterial Proteins/metabolism , High-Throughput Screening Assays , Molecular Dynamics Simulation , Small Molecule Libraries/metabolism , beta-Lactamases/metabolism , Bacterial Proteins/chemistry , Drug Evaluation, Preclinical , Escherichia coli/enzymology , Kinetics , Protein Binding , Protein Conformation , Thermodynamics , Thiophenes/metabolism , beta-Lactamases/chemistry
SELECTION OF CITATIONS
SEARCH DETAIL
...