Roy, RS and Balaram, P (2004) Conformational properties of hybrid peptides containing a- and w-amino acids. In: Journal of Peptide Research, 63 (3). pp. 279-289.
This review briefly surveys the conformational properties of guest w-amino acid residues when incorporated into host a-peptide sequences. The results presented focus primarily on the use of b- and g-residues in aw 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 a-peptides and hybrid sequences, is defined. Crystal structure determination of hybrid peptides, which adopt helical and b-hairpin conformations permits the characterization of backbone conformational parameters for b- and g-residues inserted into regular a-polypeptide structures. Substituted b- and g-residues are more limited in the range of accessible conformation than their unsubstituted counterparts. The achiral b, b-disubstituted g-amino acid, gabapentin, is an example of a stereochemically constrained residue in which the torsion angles about the C -C ( 1) and C -C ( 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 for this article belongs to Blackwell Publishing|
|Keywords:||alpha w sequences;beta-peptides;gamma-peptides;hybrid peptides;peptide conformations|
|Department/Centre:||Division of Biological Sciences > Molecular Biophysics Unit|
|Date Deposited:||26 Jul 2004|
|Last Modified:||19 Sep 2010 04:14|
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