Circular dichroism studies of helical oligopeptides. Can 3(10) and alpha-helical conformations be chiroptically distinguished?
Circular dichroism studies of seven helical oligopeptides containing alpha-aminoisobutyric acid (Aib) in methanol and trifluoroethanol (TFE) solutions are reported. Peptides ranging from 10 to 21 residues in length have been examined. In all cases distinct negative CD bands characteristic of helical peptides are obtained at approximately 220 and 205 nm corresponding to the n-pi and pi-pi transitions, respectively. The ratio R = [theta] pi-pi is less than 1.0 for all peptides studied. Using crystal structure and n.m.r. results for a 10 residue 3(10) helical peptide and literature values for an alpha-helical 11-residue peptide, it is shown that both helical conformations yield R values of approximately 0.8 in alcoholic solvents. The CD data are considered in the light of 1H n.m.r. studies on these oligopeptides. The results suggest that 3(10) and alpha-helical conformations cannot be distinguished by CD methods.
D000595:Amino Acid Sequence; D002942:Circular Dichroism / Q000379:methods; D009842:Oligopeptides / Q000138:chemical synthesis; D011487:Protein Conformation; D013329:Structure-Activity Relationship
D009842:Oligopeptides