Abstract
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
Current Medicinal Chemistry
Title:ATP Synthase: A Molecular Therapeutic Drug Target for Antimicrobial and Antitumor Peptides
Volume: 20 Issue: 15
Author(s): Zulfiqar Ahmad, Florence Okafor, Sofiya Azim and Thomas F. Laughlin
Affiliation:
Keywords: F1Fo ATP synthase, ATPase, E. coli ATP synthase, antimicrobial peptides, antitumor peptides, enzyme inhibitors
Abstract: 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.
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Cite this article as:
Ahmad Zulfiqar, Okafor Florence, Azim Sofiya and F. Laughlin Thomas, ATP Synthase: A Molecular Therapeutic Drug Target for Antimicrobial and Antitumor Peptides, Current Medicinal Chemistry 2013; 20 (15) . https://dx.doi.org/10.2174/0929867311320150003
DOI https://dx.doi.org/10.2174/0929867311320150003 |
Print ISSN 0929-8673 |
Publisher Name Bentham Science Publisher |
Online ISSN 1875-533X |
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