Conformational properties of hybrid peptides containing α- and ω-amino acids

Roy, R. S. ; Balaram, P. (2004) Conformational properties of hybrid peptides containing α- and ω-amino acids The Journal of Peptide Research, 63 (3). pp. 279-289. ISSN 1397-002X

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Official URL: http://www3.interscience.wiley.com/journal/1200934...

Related URL: http://dx.doi.org/10.1111/j.1399-3011.2004.00143.x

Abstract

This review briefly surveys the conformational properties of guest ω-amino acid residues when incorporated into host β-peptide sequences. The results presented focus primarily on the use of β- and γ-residues in αω sequences. The insertion of additional methylene groups into peptide backbones enhances the range of accessible conformations, introducing additional torsional variables. A nomenclature system, which permits ready comparisons between α-peptides and hybrid sequences, is defined. Crystal structure determination of hybrid peptides, which adopt helical and β-hairpin conformations permits the characterization of backbone conformational parameters for β- and γ-residues inserted into regular α-polypeptide structures. Substituted β- and γ-residues are more limited in the range of accessible conformation than their unsubstituted counterparts. The achiral β,β-disubstituted γ-amino acid, gabapentin, is an example of a stereochemically constrained residue in which the torsion angles about the Cβ-Cγ1) and Cα-Cβ2) bonds are restricted to the gauche conformation. Hybrid sequences permit the design of novel hydrogen bonded rings in peptide structures.

Item Type:Article
Source:Copyright of this article belongs to John Wiley and Sons, Inc.
Keywords:αω Sequences; β-peptides; γ-peptides; Hybrid Peptides; Peptide Conformations
ID Code:4507
Deposited On:18 Oct 2010 07:39
Last Modified:16 May 2016 15:09

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