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

Authors
Journal
Peptides
0196-9781
Publisher
Elsevier
Publication Date
Volume
10
Issue
2
Identifiers
DOI: 10.1016/0196-9781(89)90042-9
Keywords
  • Melanin Concentrating Hormone (Mch)
  • Analogue Synthesis
  • Analogue Fragments
  • Synbranchus Marmoratus
  • Fish Skin Bioassay

Abstract

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 Trp 15, 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 Trp 15 residue for interaction with the MCH receptor in this assay system.

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