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Medicinal chemistry of ATP synthase: a potential drug target of dietary polyphenols and amphibian antimicrobial peptides.

机译:ATP合酶的药物化学:膳食多酚和两栖抗菌肽的潜在药物靶标。

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In this review we discuss the inhibitory effects of dietary polyphenols and amphibian antimicrobial/antitumor peptides on ATP synthase. In the beginning general structural features highlighting catalytic and motor functions of ATP synthase will be described. Some details on the presence of ATP synthase on the surface of several animal cell types, where it is associated with multiple cellular processes making it an interesting drug target with respect to dietary polyphenols and amphibian antimicrobial peptides will also be reviewed. ATP synthase is known to have distinct polyphenol and peptide binding sites at the interface of alpha/beta subunits. Molecular interaction of polyphenols and peptides with ATP synthase at their respective binding sites will be discussed. Binding and inhibition of other proteins or enzymes will also be covered so as to understand the therapeutic roles of both types of molecules. Lastly, the effects of polyphenols and peptides on the inhibition of Escherichia coli cell growth through their action on ATP synthase will also be presented.
机译:在这篇综述中,我们讨论了膳食多酚和两栖抗微生物/抗肿瘤肽对ATP合酶的抑制作用。首先,将描述突出ATP合酶催化和运动功能的一般结构特征。还将审查几种动物细胞表面上ATP合酶的存在的一些细节,其中与多种细胞过程有关,这使其成为饮食中多酚和两栖抗菌肽的有趣药物靶标。已知ATP合酶在α/β亚基的界面上具有独特的多酚和肽结合位点。将讨论多酚和多肽与ATP合酶在其各自结合位点的分子相互作用。也将涵盖对其他蛋白质或酶的结合和抑制,以了解这两种分子的治疗作用。最后,还将介绍多酚和多肽通过其对ATP合酶的作用对大肠杆菌细胞生长的抑制作用。

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