Binding and biological activity of C-terminally modified melanocortin peptides: a comparison between their actions at rodent MC1 and MC3 receptors

Peptides. 1997;18(7):1001-8. doi: 10.1016/s0196-9781(97)00035-1.


Five subtypes of melanocortin receptors have to date been identified, but to date little is known about the different structural requirements for binding and biological activity at these receptors. In this study, the role of C-terminal melanocortin peptide residues in imparting selectivity for the receptor subtypes was examined. C-terminally modified analogues of alpha-MSH and gamma-MSH were synthesized and their interaction with MC1 and MC3 melanocortin receptors was investigated. This study provides further evidence for an important role of proline 12 (numbering with respect to alpha-MSH) for binding and activity at the MC1 receptor. Although the influence of C-terminal amino acids on binding and activity at MC3-R was less marked, some of them were nevertheless observed to be beneficial for the interaction with this receptor subtype.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence
  • Animals
  • Binding Sites
  • Binding, Competitive
  • Cell Line
  • Humans
  • Kinetics
  • Melanocyte-Stimulating Hormones / chemistry
  • Melanocyte-Stimulating Hormones / metabolism*
  • Melanocyte-Stimulating Hormones / pharmacology*
  • Mice
  • Molecular Sequence Data
  • Rats
  • Receptor, Melanocortin, Type 3
  • Receptors, Corticotropin / drug effects*
  • Receptors, Corticotropin / genetics
  • Receptors, Corticotropin / metabolism*
  • Receptors, Melanocortin
  • Structure-Activity Relationship
  • Transfection
  • alpha-MSH / analogs & derivatives
  • alpha-MSH / metabolism
  • alpha-MSH / pharmacology


  • Mc3r protein, mouse
  • Receptor, Melanocortin, Type 3
  • Receptors, Corticotropin
  • Receptors, Melanocortin
  • alpha-MSH
  • Melanocyte-Stimulating Hormones