Conformation control of abiotic α-helical foldamers.
J Chem Inf Model
; 53(10): 2671-80, 2013 Oct 28.
Article
en 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
Banco de datos:
MEDLINE
Asunto principal:
Piridinas
/
Proteínas
/
Bibliotecas de Moléculas Pequeñas
Idioma:
En
Año:
2013
Tipo del documento:
Article