Ribbon structure stabilized by C10 and C12 turns in αγ hybrid peptide.
J Pept Sci
; 22(4): 208-13, 2016 Apr.
Article
em En
| MEDLINE
| ID: mdl-27028205
ABSTRACT
The present study describes the synthesis and crystallographic analysis of αγ hybrid peptides, Boc-Gpn-L-Pro-NHMe (1), Boc-Aib-Gpn-L-Pro-NHMe (2), and Boc-L-Pro-Aib-Gpn-L-Pro-NHMe (3). Peptides 1 and 2 adopt expanded 12-membered (C12 ) helical turn over γα segment. Peptide 3 promotes the ribbon structure stabilized by type II ß-turn (C10 ) followed by the expanded C12 helical γα turn. Both right-handed and left-handed helical conformations for Aib residue are observed in peptides 2 and 3, respectively.
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01-internacional
Base de dados:
MEDLINE
Assunto principal:
Oligopeptídeos
Idioma:
En
Ano de publicação:
2016
Tipo de documento:
Article