Conformation Control of Abiotic α-Helical Foldamers

被引：7

作者：

Perato, Serge ^{[1
]}

Fogha, Jade ^{[1
]}

Sebban, Muriel ^{[2
]}

Voisin-Chiret, Anne Sophie ^{[1
]}

Santos, Jana Sopkova-de Oliveira ^{[1
]}

Oulyadi, Hassan ^{[2
]}

Rault, Sylvain ^{[1
]}

机构：

[1] UNICAEN, CERMN, UPRES EA 4258, INC3M,FR CNRS 3038, F-14032 Caen, France

[2] Univ Rouen, COBRA UMR 6014, F-76821 Mont St Aignan, France

来源：

JOURNAL OF CHEMICAL INFORMATION AND MODELING | 2013年 / 53卷 / 10期

关键词：

PROTEIN-PROTEIN INTERACTIONS; MIMETICS; MIMICS; DESIGN;

D O I：

10.1021/ci400365y

中图分类号：

R914 [药物化学];

学科分类号：

100701 ;

摘要：

With the aim to find new protein protein inhibitors, a three part methodology was applied to oligophenylpyridines. Theoretical ring twist angle predictions have been validated by X-ray diffraction and molecular dynamics simulations with NMR constraints. Careful choice of substituent and nitrogen positions in oligophenylpyridyl foldamer units opens the way to conformational control of the side chain distribution of this alpha-helix mimic.

引用

页码：2671 / 2680

页数：10

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