Conformation control of abiotic α-helical foldamers.
J Chem Inf Model
; 53(10): 2671-80, 2013 Oct 28.
Article
em En
| MEDLINE
| ID: mdl-24032461
ABSTRACT
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 α-helix mimic.
Texto completo:
1
Base de dados:
MEDLINE
Assunto principal:
Piridinas
/
Proteínas
/
Bibliotecas de Moléculas Pequenas
Idioma:
En
Revista:
J Chem Inf Model
Assunto da revista:
INFORMATICA MEDICA
/
QUIMICA
Ano de publicação:
2013
Tipo de documento:
Article
País de afiliação:
França