Structure-activity relationships of a pigment-dispersing crustacean neurohormone

• Published in: Peptides (New York, N.Y. : 1980) Vol. 3; no. 4; p. 643
• Main Authors: Riehm, J P, Rao, K R
• Format: Journal Article
• Language: English
• Published: United States 01-01-1982
• Subjects: Amino Acid Sequence; Animals; Biological Assay; Brachyura; Chemical Phenomena; Chemistry; Crustacea; Melanophores - drug effects; Melanophores - metabolism; Peptides - pharmacology; Retinal Pigments - metabolism; Structure-Activity Relationship
• DOI: 10.1016/0196-9781(82)90165-6
• ISSN: 0196-9781

This study evaluated the effects of N-terminal sequence deletion and of chemical modifications on the melanophore pigment dispersing activity of a crustacean neuropeptide (DRPH: Asn-Ser-Gly-Met-Ile-Asn-Ser-Ile-Leu-Gly-Ile-Pro-Arg-Val-Met-Thr-Glu-Ala-NH2). Sustained biological activity was not demonstrated by peptides smaller than the tridecapeptide DRPH (6-18). N-terminal extension of this peptide led to a steady increase in activity, with the DRPH (1-18) showing the maximum activity. Carboxyl group modification had no effect, but acetylation, oxidation, cyanogen bromide, and trypsin caused a decrease in activity. Phenylglyoxal modification of Arg-13 in DRPH led to a 14-fold increase in activity. It is concluded that the N-terminus and the methionine residues are important for full activity and that the phenylglyoxal-induced potentiation is due to protection of the peptide from proteolysis in vivo.