Mark ShepherdLAMA YOUSEF ALAJLAN2022-05-292022-05-29https://drepo.sdl.edu.sa/handle/20.500.14154/45964Antibiotic 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.enDrug repurposing approaches to combat antibiotic-resistant E. coli infections