Potent and prolonged melanotropic activities of the α-MSH fragment analog, Ac-[Nle4, D-Phe7]-α-MSH4-9-NH2

David G. Klemes, Kristie L. Kreutzfeld, Mac E. Hadley, Wayne L. Cody, Victor J. Hruby

Research output: Contribution to journalArticlepeer-review

9 Scopus citations

Abstract

Ac-[Nle4, D-Phe7]-α-MSH4-9-NH2 and Ac-[Nle4]-α-MSH4-9-NH2, fragment analogs of the tridecapeptide, α-melanocyte stimulating hormone (α-MSH, α-melanotropin), were synthesized. The potency and prolonged activity of the analogs were compared to α-MSH in several melanotropin bioassays. The D-Phe-containing hexapeptide was 10 times more active than α-MSH in stimulating melanoma tyrosinase activity. This analog was also 10-fold more potent than α-MSH in the lizard skin bioassay and about 10-fold less active in the frog skin bioassay. The melanotropic activity of Ac-[Nle4, D-Phe7]-α-MSH4-9-NH2 was considerably prolonged compared to α-MSH in each of the bioassays. These results demonstrate that the structural requirements for superpotency and prolonged activity of [Nle4, D-Phe7]-substituted analogs reside within this hexapeptide sequence.

Original languageEnglish (US)
Pages (from-to)722-728
Number of pages7
JournalBiochemical and Biophysical Research Communications
Volume137
Issue number2
DOIs
StatePublished - Jun 13 1986

ASJC Scopus subject areas

  • Biophysics
  • Biochemistry
  • Molecular Biology
  • Cell Biology

Fingerprint Dive into the research topics of 'Potent and prolonged melanotropic activities of the α-MSH fragment analog, Ac-[Nle<sup>4</sup>, D-Phe<sup>7</sup>]-α-MSH<sub>4-9</sub>-NH<sub>2</sub>'. Together they form a unique fingerprint.

Cite this