Melanin concentrating hormone (MCH): Synthesis and bioactivity studies of MCH fragment analogues

Terry O. Matsunaga, Ana Maria De Lauro Castrucci, Mac E. Hadley, Victor J. Hruby

Research output: Contribution to journalArticle

20 Scopus citations

Abstract

Nineteen analogues of melanin concentrating hormone (MCH) were synthesized and tested for their skin-lightening activities in the in vitro eel skin (Synbranchus marmoratus) bioassay. All the analogues synthesized were fragments of the native sequence: Asp-Thr-Met-Arg-Cys-Met-Val-Gly-Arg-Val-Tyr-Arg-Pro-Cys-Trp-Glu-Val with sequential elimination of substituents from both the carboxy- and amino-termini. All the analogues that contained trytophan in position 15 were found to be full agonists and equipotent to MCH. In the absence of Trp15, full agonist activity was maintained but potency was reduced ten-fold or more. The minimal fragment analogue possessing equipotency to the parent peptide, MCH, was the MCH(5-15) sequence. These observations coupled with results from work reported previously by our laboratories suggest the importance of the Trp15 residue for interaction with the MCH receptor in this assay system.

Original languageEnglish (US)
Pages (from-to)349-354
Number of pages6
JournalPeptides
Volume10
Issue number2
DOIs
StatePublished - Jan 1 1989

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Keywords

  • Analogue fragments
  • Analogue synthesis
  • Fish skin bioassay
  • Melanin concentrating hormone (MCH)
  • Synbranchus marmoratus

ASJC Scopus subject areas

  • Biochemistry
  • Physiology
  • Endocrinology
  • Cellular and Molecular Neuroscience

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