In this review we discuss the role of ATP synthase as a molecular drug target for natural and synthetic antimicrobial/
antitumor peptides. We start with an introduction of the universal nature of the ATP synthase enzyme and its role
as a biological nanomotor. Significant structural features required for catalytic activity and motor functions of ATP synthase
are described. Relevant details regarding the presence of ATP synthase on the surface of several animal cell types,
where it is associated with multiple cellular processes making it a potential drug target with respect to antimicrobial peptides
and other inhibitors such as dietary polyphenols, is also reviewed. ATP synthase is known to have about twelve discrete
inhibitor binding sites including peptides and other inhibitors located at the interface of α/β subunits on the F1 sector
of the enzyme. Molecular interaction of peptides at the β DEELSEED site on ATP synthase is discussed with specific examples.
An inhibitory effect of other natural/synthetic inhibitors on ATP is highlighted to explore the therapeutic roles
played by peptides and other inhibitors. Lastly, the effect of peptides on the inhibition of the Escherichia coli model system
through their action on ATP synthase is presented.
Keywords: F1Fo ATP synthase, ATPase, E. coli ATP synthase, antimicrobial peptides, antitumor peptides, enzyme inhibitors
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