Exploration of α/ß/γ-peptidomimetics design for BH3 helical domains.
Chem Commun (Camb)
; 58(7): 945-948, 2022 Jan 20.
Article
in En
| MEDLINE
| ID: mdl-34985060
ABSTRACT
Systematic incorporation of ring-constrained ß- and γ-amino acid residues into α-helix mimetics engenders stable helical secondary structures. In this paper, functional α/ß/γ-helical peptidomimetics were explored for mimicry of BH3 helical domains, Bim as a pioneering study. The Bim-based α/ß/γ-peptides in an αγααßα-hexad repeat with five helical turns inhibited the interaction between Bak and Bcl-xL with excellent resistance towards proteolytic digestion. Further optimization of the α/ß/γ-backbone strategy will considerably expand the utility of functional α/ß/γ-peptidomimetics, in particular due to its prominent stability against proteolysis.
Full text:
1
Collection:
01-internacional
Database:
MEDLINE
Main subject:
Peptidomimetics
Language:
En
Journal:
Chem Commun (Camb)
Journal subject:
QUIMICA
Year:
2022
Document type:
Article
Affiliation country:
United States