Turn residues in beta-hairpin peptides as points for covalent modification.
Beta-turns are important sites for protein-protein and protein-peptide interactions, but little research has explored synthetic modifications of turn residue side-chains in a beta-hairpin peptide. To this end, beta-hairpin peptides were synthesized containing the type I' turn sequence Val-Asn-Gly-Lys with modifications at Asn and Lys. We found that these variations impose a small penalty, demonstrating that beta-turns are capable of displaying a range of functionality, which may be exploited for biomolecular recognition and medicinal applications. [structure: see text]
Cooper
W John
WJ
Department of Chemistry, CB 3290, University of North Carolina, Chapel Hill, NC 27599, USA.
Waters
Marcey L
ML
D000595:Amino Acid Sequence; D001216:Asparagine / Q000737:chemistry; D008958:Models, Molecular; D015394:Molecular Structure; D010455:Peptides / Q000138:chemical synthesis* / Q000737:chemistry*; D011487:Protein Conformation; D017510:Protein Folding; D017433:Protein Structure, Secondary
D010455:Peptides; D001216:Asparagine