Structural effects of glycosylation on the C-terminal pentapeptide of peptide T.
Structural effects of glycosylation of the C-terminal pentapeptide fragment of Peptide T (Thr-Thr-Asn-Tyr-Thr) were studied. Because of the inherent flexibility of these molecules, molecular simulations are used to interpret the circular dichroism and nuclear magnetic resonance data acquired for these molecules. N-acetyl-glucosamine attached at the Asn residue changes the ensemble average backbone conformation of the peptide and limits the conformational space available to the pentapeptide fragment. Glycosylation changes the type I and III beta-turn propensity of the pentapeptide to a type II turn. Since glycosylation also increases peptide solubility and inhibits peptide degradation in human serum, glycopeptide design may be an efficient approach to stabilize or conformationally modify peptide drug candidates and to create additional diversity in peptide libraries.
Prammer
K V
KV
Wistar Institute, Philadelphia, PA 19104, USA.
Otvos
L
L
D000117:Acetylglucosamine; D000595:Amino Acid Sequence; D001216:Asparagine; D002942:Circular Dichroism; D003198:Computer Simulation; D006031:Glycosylation; D006801:Humans; D008958:Models, Molecular; D019906:Nuclear Magnetic Resonance, Biomolecular; D010446:Peptide Fragments / Q000737:chemistry*; D019151:Peptide Library; D015717:Peptide T / Q000097:blood / Q000737:chemistry*; D011487:Protein Conformation; D017433:Protein Structure, Secondary
D010446:Peptide Fragments; D019151:Peptide Library; D015717:Peptide T; D001216:Asparagine; D000117:Acetylglucosamine