Unexpected binding modes of inhibitors to the histone chaperone ASF1 revealed by a foldamer scanning approach.
Chem Commun (Camb)
; 59(56): 8696-8699, 2023 Jul 11.
Article
em En
| MEDLINE
| ID: mdl-37347155
ABSTRACT
In the search for foldamer inhibitors of the histone chaperone ASF1, we explored the possibility of substituting four α-residues (≈one helix turn) by 3-urea segments and scanned the sequence of a short α-helical peptide known to bind ASF1. By analysing the impact of the different foldamer replacements within the peptide chain, we uncovered new binding modes of the peptide-urea chimeras to ASF1.
Texto completo:
1
Base de dados:
MEDLINE
Assunto principal:
Histonas
/
Chaperonas de Histonas
Idioma:
En
Ano de publicação:
2023
Tipo de documento:
Article