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Structure-activity relationship studies for inhibitors for vancomycin-resistant and human carbonic anhydrases

J Enzyme Inhib Med Chem. 2022-12; 
Weiwei An, Katrina J Holly, Alessio Nocentini, Ryan D Imhoff, Chad S Hewitt, Nader S Abutaleb, Xufeng Cao, Mohamed N Seleem, Claudiu T Supuran, Daniel P Flaherty
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Vancomycin-resistant enterococci (VRE), consisting of pathogenic , is a leading cause of hospital-acquired infections (HAIs). We recently repurposed the FDA-approved human carbonic anhydrase (CA) inhibitor acetazolamide () against VRE agent with the likely mechanism of action for the molecules being inhibition of one, or both, of the bacterial CA isoforms expressed in VRE. To elucidate how inhibitor binding to the enzymes relates to MIC, we further characterised the inhibition constants () against the α-CA (-CA) and γ-CA (γ-CA), as well as against human CA I (hCAI) and human CA II (hCAII) to assess selectivity. We have also utilised homology modelling and molecular dynamics (MD) simulations to gain a better... More


Carbonic anhydrase inhibitors, antibiotics, drug repurposing, vancomycin-resistant Enterococcus