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Melanotan-I

Afamelanotide, MT-I, [Nle4-D-Phe7]-α-MSH, Scenesse, CUV-1647

Quick Stats
Studies 225
Trials 100
Overview Studies Clinical Trials
Score 3
1984 pubmed 43 citations

Enzymological studies of melanotropins.

Castrucci. A M AM; Hadley. M E ME; Sawyer. T K TK; Hruby. V J VJ

View on DOI View Original Source

Key Findings

  • Natural alpha‑ and beta‑MSH are rapidly inactivated by serum enzymes, especially frog serum
  • Synthetic analogues like [Nle4, D‑Phe7]‑alpha‑MSH (melanotan‑I) are resistant to serum proteolysis
  • Synthetic analogues also show resistance to digestive enzymes like chymotrypsin and trypsin

Practical Outcomes

  • For biohackers, this confirms that melanotan‑I is stable enough for subcutaneous or intranasal use, so dosing schedules don’t need to account for rapid degradation. It also suggests that natural MSH supplements would be ineffective due to quick breakdown, reinforcing the preference for the synthetic analogue.

Summary

The study shows that natural melanotropins (alpha‑ and beta‑MSH) are quickly broken down by enzymes in blood, especially in frogs, while the synthetic version used in melanotan‑I ([Nle4, D‑Phe7]‑alpha‑MSH) is highly resistant to this breakdown. This means the synthetic peptide stays active longer in the body, making it more useful for research or self‑experiments compared to the natural hormones.

Abstract

The relative stability of natural melanotropins and related synthetic analogues to serum and purified proteolytic enzymes was studied. Both alpha- and beta-MSH were rapidly inactivated by frog serum, but much more slowly by rat serum. beta-MSH was more stable than alpha-MSH to serum inactivation. Both alpha- and beta-MSH were rapidly inactivated by alpha-chymotrypsin and trypsin. The synthetic analogues, [Nle4, D-Phe7]-alpha-MSH and [Cys4, Cys10]-alpha-MSH, were totally resistant to inactivation by frog and rat serum enzymes. [Nle4, D-Phe7]-alpha-MSH was resistant to inactivation by alpha-chymotrypsin and trypsin, whereas [Cys4, Cys10]-alpha-MSH was partially resistant to these enzymes under similar conditions. Melanotropin analogues resistant to inactivation by serum enzymes may prove useful in a variety of physiological studies wherein natural melanotropins would be rapidly inactivated.

Study Information

Provider

pubmed

Year

1984

DOI

10.1016/0305-0491(84)90090-7

Citations

43

References

15