Opioid peptides. Conformational studies of dermorphin and its constitutive fragments by circular dichroism. IX.
Dermorphins are potent opiate-like heptapeptides which have been isolated from the skin of South American frogs. The Circular Dichroism spectra carried out on dermorphin (Tyr-D-Ala-Phe-Gly-Tyr-Pro-Ser-NH2), on the analogous [L-Ala2] dermorphin and on N-terminal fragments suggest that, in solution, the native molecule possesses a peculiar folded conformation responsible for its pharmacological activity. The presence of alanine in D configuration and of aminoacid residues possessing a high "beta-turn" potential, seems to be the main reason for such active conformation.
D000595:Amino Acid Sequence; D002942:Circular Dichroism; D004723:Endorphins / Q000032:analysis*; D009842:Oligopeptides / Q000032:analysis*; D018847:Opioid Peptides; D010446:Peptide Fragments; D011487:Protein Conformation; D013056:Spectrophotometry, Ultraviolet
D004723:Endorphins; D009842:Oligopeptides; D018847:Opioid Peptides; D010446:Peptide Fragments; C030058:dermorphin