Comparative α-helicity of cyclic pentapeptides in water.
Angew Chem Int Ed Engl
; 53(27): 6965-9, 2014 Jul 01.
Article
in En
| MEDLINE
| ID: mdl-24828311
ABSTRACT
Helix-constrained polypeptides have attracted great interest for modulating protein-protein interactions (PPI). It is not known which are the most effective helix-inducing strategies for designing PPI agonists/antagonists. Cyclization linkers (X1-X5) were compared here, using circular dichroism and 2D NMR spectroscopy, for α-helix induction in simple model pentapeptides, Ac-cyclo(1,5)-[X1-Ala-Ala-Ala-X5]-NH2, in water. In this very stringent test of helix induction, a Lys1âAsp5 lactam linker conferred greatest α-helicity, hydrocarbon and triazole linkers induced a mix of α- and 310-helicity, while thio- and dithioether linkers produced less helicity. The lactam-linked cyclic pentapeptide was also the most effective α-helix nucleator attached to a 13-residue model peptide.
Key words
Full text:
1
Collection:
01-internacional
Database:
MEDLINE
Main subject:
Oligopeptides
/
Peptides, Cyclic
/
Water
Language:
En
Journal:
Angew Chem Int Ed Engl
Year:
2014
Document type:
Article