Drug repurposing approaches to combat antibiotic-resistant E. coli infections

Abstract

Antibiotic resistance Escherichia coli (E.coli) is an increasing global challenge with devastating impact on public health, leading to urgent requirements to repurposing older drugs and re-evaluating many abandoned compounds using modern methods to tackle this crises. Other studies have extensively investigated the respiratory chain of E.coli as a potential alternative drug target. The membrane protein formate dehydrogenase (Fdn), a major component of E.coli respiration chain, provides critical input to proton motive force generation by transferring electrons from formate to the quinone pool. A PDB crystallised structure of Fdn (1KQG) was used for molecular docking and computational analyses to investigate a library of 50 FDA-approved inhibitors that were implicated to bind to the quinol binding cleft of cytochrome bd in Shepherd lab, University of Kent.