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

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

DOI:
10.2174/092986710791859270
复制
发表时间:
2010
影响因子:
4.1
通讯作者:
Laughlin TF
Laughlin TF
中科院分区:
医学3区
文献类型:
--
作者:
Ahmad Z;Laughlin TF

文献摘要

被引文献

相似文献

本文就多酚类化合物和两栖类抗菌/抗肿瘤肽对ATP合成酶的抑制作用进行综述。在开始时,一般的结构特点突出的催化和电机功能的ATP合酶将被描述。一些细节上的存在下的ATP合酶的表面上的几种动物细胞类型,在那里它是与多个细胞过程,使其成为一个有趣的药物靶点,相对于饮食多酚和两栖动物抗菌肽也将进行审查。已知ATP合酶在α/β亚基的界面处具有不同的多酚和肽结合位点。多酚和肽与ATP合酶在各自的结合位点的分子相互作用将被讨论。其他蛋白质或酶的结合和抑制也将包括在内,以了解这两种类型的分子的治疗作用。最后,还将介绍多酚和肽通过其对ATP合酶的作用对大肠杆菌细胞生长的抑制作用。
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 α/β 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.