Roy, RS and Balaram, Padmanabhan (2004) Conformational properties of hybrid peptides containing alpha and omega-amino acids. In: The Journal of Peptide Research, 63 (3). pp. 279-289.
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This review briefly surveys the conformational properties of guest omega-amino acid residues when incorporated into host alpha-peptide sequences. The results presented focus primarily on the use of beta- and gamma-residues in alphaomega 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 alpha-peptides and hybrid sequences, is defined. Crystal structure determination of hybrid peptides, which adopt helical and beta-hairpin conformations permits the characterization of backbone conformational parameters for beta- and gamma-residues inserted into regular alpha-polypeptide structures. Substituted beta- and gamma-residues are more limited in the range of accessible conformation than their unsubstituted counterparts. The achiral beta,beta-disubstituted gamma-amino acid, gabapentin, is an example of a stereochemically constrained residue in which the torsion angles about the C-beta-C-gamma (theta(1)) and C-alpha-C-beta (theta(2)) bonds are restricted to the gauche conformation. Hybrid sequences permit the design of novel hydrogen bonded rings in peptide structures.
|Item Type:||Journal Article|
|Additional Information:||Copyright of this article belongs to John Wiley & Sons.|
|Keywords:||alpha omega sequences; beta-peptides; gamma-peptides; hybrid peptides; peptide conformations|
|Department/Centre:||Division of Biological Sciences > Molecular Biophysics Unit|
|Date Deposited:||24 Nov 2010 08:39|
|Last Modified:||24 Nov 2010 08:39|
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