Inhibition of the Clathrin Terminal Domain-Amphiphysin Protein-Protein Interaction. Probing the Pitstop 2 Aromatic Moiety

抑制网格蛋白末端结构域-两亲蛋白相互作用。探究Pitstop 2芳香部分

阅读:4

Abstract

Pitstop 2, (Z)-N-(5-(4-bromenzylidene)-4-oxo-4,5-dihydrothiazol-2-yl)naphthalene-1-sulfonamide (1) inhibits the clathrin terminal domain-amphiphysin interaction (NTD-PPI) and has been widely used to investigate endocytosis. Herein, the synthesis of 56 novel Pitstop 2 analogues via four discrete focused libraries is reported. Specific modification to the 4-bromonenzylidene moiety is explored, and their ability to inhibit the NTD-PPI interaction is examined by ELISA. In cell endocytosis, effects are measured for selective analogues as is the inhibition of dynamin, another protein involved in the endocytosis process. The most NTD-PPI active analogues retain 2- and 4-disposed substituents on the aromatic head, with 2,3,4-trihydroxy (28) the most active (IC(50) 0.94 μm). Catechol-free 2,3-dihydroxybenzo[b][1,4]dioxone (54) is a more promising lead with an NTD-PPI IC(50) = 1.16 μm. The corresponding benzo[d][1,3]dioxole (53) is threefold less active suggesting ring size preference at this position. Nine analogues show improved or comparable NTD-PPI activity to Pitstop 2 with IC(50) values from 0.94 to 2.1 μM. Heterocyclic analogues are well tolerated and potent inhibitors of CME in U2OS cells, in particular, benzofuran 67 (NTD-PPI IC(50) 1.5 μm and CME IC(50) 6.8 ± 2.7 μm). This positions 67 as one of the most cell active inhibitors of clathrin-mediated endocytosis yet reported.

特别声明

1、本页面内容包含部分的内容是基于公开信息的合理引用;引用内容仅为补充信息,不代表本站立场。

2、若认为本页面引用内容涉及侵权,请及时与本站联系,我们将第一时间处理。

3、其他媒体/个人如需使用本页面原创内容,需注明“来源:[生知库]”并获得授权;使用引用内容的,需自行联系原作者获得许可。

4、投稿及合作请联系:info@biocloudy.com。