期刊
JOURNAL OF PEPTIDE SCIENCE
卷 17, 期 4, 页码 288-296出版社
WILEY
DOI: 10.1002/psc.1337
关键词
Freidinger lactams; beta-amino gamma-lactam; lactam scanning; interleukin-1 receptor; 101.10; CD; peptide mimic; beta-turn; conformational analysis; solid-phase peptide synthesis
资金
- Natural Sciences and Engineering Research Council of Canada (NSERC)
- Universite de Montreal
- Canadian Institutes of Health Research CIHR-Team in GPCR allosteric regulation (CTiGAR) [CIP-79848]
- Canadian Institutes of Health Research
- Fonds Quebecois de la Recherche sur la Nature et les Technologies (FQRNT)
- Ministere du Developpement Economique, de l'Innovation et de l'Exportation du Quebec
- Fonds de Recherche en Sante du Quebec
- Reseau de Recherche en Sante de la Vision
The relationship between the conformation and biological activity of the peptide allosteric modulator of the interleukin-1 receptor 101.10 (D-Arg-D-Tyr-D-Thr-D-Val-D-Glu-D-Leu-D-Ala-NH2) has been studied using (R)- and (S)-Bgl residues. Twelve Bgl peptides were synthesized using (R)- and (S)-cyclic sulfamidate reagents derived from L-and D-aspartic acid in an optimized Fmoc-compatible protocol for efficient lactam installment onto the supported peptide resin. Examination of these (R)- and (S)-Bgl 101.10 analogs for their potential to inhibit IL-1 beta-induced thymocyte cell proliferation using a novel fluorescence assay revealed that certain analogs exhibited retained and improved potency relative to the parent peptide 101.10. In light of previous reports that Bgl residues may stabilize type II' beta-turn-like conformations in peptides, CD spectroscopy was performed on selected compounds to identify secondary structure necessary for peptide biological activity. Results indicate that the presence of a fold about the central residues of the parent peptide may be important for activity. Copyright (C) 2011 European Peptide Society and John Wiley & Sons, Ltd.
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