The effect of N-terminal substitutions on the biological activity of MSH fragments

H. Süli-Vargha, J. Bódi, H. Medzihradszky-Schweiger, K. Medzihradszky

Research output: Contribution to journalArticle

3 Citations (Scopus)

Abstract

In order to study the role of N-terminal substitutions of peptide sequences related to the active site of α-melanotropin, [Glp5]α-MSH(5-10), [Glp5,d-Phe7]α-MSH(5-10), [Sar5,d-Phe7]α-MSH(5-10), [Nle4,d-Phe7]α-MSH(4-10), [N-carbamoyl]α-MSH(5-10), and formyl and acetyl derivatives of α-MSH(5-10), [Gly5]α-MSH(5-10) and [Gly5,d-Phe7]α-MSH(5-10), were synthesized in solution. The N-terminal acylations enhance by 2 to 10 times the melanin-dispersing activity of the unsubstituted sequences. Alkylation of the N-terminus does not change the biological activity of the parent peptide, suggesting the necessity of a carbonyl group for increasing the hormonal effect.

Original languageEnglish
Pages (from-to)1145-1148
Number of pages4
JournalPeptides
Volume13
Issue number6
DOIs
Publication statusPublished - Jan 1 1992

    Fingerprint

Keywords

  • Biological activity
  • Melanotropin fragments
  • N-acyl peptides
  • N-alkyl peptide
  • Synthesis

ASJC Scopus subject areas

  • Biochemistry
  • Physiology
  • Endocrinology
  • Cellular and Molecular Neuroscience

Cite this