Macrocyclization of an all-d linear α-helical peptide imparts cellular permeability.
Journal
Chemical science
ISSN: 2041-6520
Titre abrégé: Chem Sci
Pays: England
ID NLM: 101545951
Informations de publication
Date de publication:
07 Jun 2020
07 Jun 2020
Historique:
received:
17
12
2019
accepted:
08
05
2020
entrez:
3
9
2020
pubmed:
3
9
2020
medline:
3
9
2020
Statut:
epublish
Résumé
Peptide-based molecules hold great potential as targeted inhibitors of intracellular protein-protein interactions (PPIs). Indeed, the vast diversity of chemical space conferred through their primary, secondary and tertiary structures allows these molecules to be applied to targets that are typically deemed intractable
Identifiants
pubmed: 32874502
doi: 10.1039/c9sc06383h
pii: c9sc06383h
pmc: PMC7441689
doi:
Types de publication
Journal Article
Langues
eng
Pagination
5577-5591Informations de copyright
This journal is © The Royal Society of Chemistry 2020.
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