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Semax

ACTH(4-10) analogue, Heptapeptide SEMAX

Quick Stats
Studies 172
Trials 37
Score 3
1993 pubmed 18 citations

Degradation of ACTH/MSH(4-10) and its synthetic analog semax by rat serum enzymes: an inhibitor study.

Potaman. V N VN; Alfeeva. L Y LY; Kamensky. A A AA; Nezavibatko. V N VN

Key Findings

  • Aminopeptidases account for the biggest part of semax degradation in rat serum (up to 66% inhibition with bestatin).
  • ACE also contributes to semax breakdown, with about 15% inhibition using lisinopril.
  • Neutral endopeptidase and prolyl endopeptidase have a minor or unclear role in semax hydrolysis.

Practical Outcomes

  • For biohackers, this suggests that semax may have a short half‑life in the bloodstream and that co‑taking an ACE inhibitor could modestly extend its activity. Strong inhibition with bestatin isn’t practical for humans, so protecting semax from aminopeptidases (e.g., via formulation or delivery method) is a more realistic strategy.

Summary

The study shows that in rat blood, the peptide semax is mainly broken down by enzymes called aminopeptidases and the angiotensin‑converting enzyme (ACE). Inhibiting these enzymes slowed the breakdown, especially with a drug called bestatin, while an ACE blocker (lisinopril) gave a smaller effect. Other enzymes seemed less important.

Abstract

Degradation of the behaviorally active peptide ACTH/MSH(4-10) and its synthetic analog semax was studied in serum in the presence of several specific peptidase inhibitors. Bestatin and puromycin were used to inhibit aminopeptidase activity, lisinopril for angiotensin-converting enzyme, phosphoramidon for neutral endopeptidase 24.11, and Z-Pro-prolinal for prolyl endopeptidase. Bestatin inhibited up to 66%, puromycin about 33%, and lisinopril about 15% of total degrading activity against both ACTH/MSH(4-10) and semax. Involvement of neutral endopeptidase and prolyl endopeptidase in hydrolysis of the two peptides was less definitive. These studies showed that aminopeptidases and angiotensin-converting enzyme are responsible for the major part of the hydrolysis of ACTH/MSH(4-10) and semax in rat serum.

Study Information

Provider

pubmed

Year

1993

Date

1993-05-01T00:00:00.000Z

DOI

10.1016/0196-9781(93)90137-6

Citations

18

References

30