[Proteolysis of simple glyprolines by leucine aminopeptidase and enzymes from nasal slime, brain membranes, and rat blood].
Shevchenko. K V KV; V'iunova. T V TV; Nagaev. I Iu IIu; Andreeva. L A LA; Miasoedov. N F NF
Key Findings
- Semax is considerably less stable to proteolysis than Pro‑Gly‑Pro‑Leu, Pro‑Gly‑Pro‑Gly, and Pro‑Gly‑Pro
- Enzymes tested included leucine aminopeptidase, nasal slime, brain microsomal fractions, and rat blood
- The primary metabolite of semax after proteolysis is His‑Phe‑Pro‑Gly‑Pro
Practical Outcomes
- Because semax degrades faster, users may need to consider protective delivery methods (e.g., enzyme inhibitors, encapsulation) or adjust dosing for nasal use. The more stable short gly‑pro peptides could be explored as alternative or adjunct compounds for similar goals.
Summary
The study compared how fast semax and three short gly‑pro‑line peptides are broken down by various enzymes. It found the short peptides are much more resistant, while semax is broken down quickly, mainly into a His‑Phe‑Pro‑Gly‑Pro fragment. This suggests semax may have limited stability when used nasally, which could affect dosing or formulation for biohackers.
Abstract
Proteolysis of Pro-Gly-Pro-Leu, Pro-Gly-Pro-Gly and Pro-Gly-Pro were studied comparatively to Met-Glu-His-Phe-Pro-Gly-Pro (semax). It is shown that all three peptides are considerably more stable to proteolysis by N-leucine-aminopeptidase (EC 3.4.11.1, Sigma, type VI, 9.2 units/mg), and by enzymes of nasal slime, brain microsomal fractions, and rat blood. Metabolites of the proteolysis showed that semax derives His-Phe-Pro-Gly-Pro only, Pro-Gly-Pro-Leu forms Gly-Pro-Leu, Pro-Gly-Pro and Gly-Pro, Pro-Gly-Pro-Gly gives Pro-Gly-Pro and Gly-Pro, and Pro-Gly-Pro forms Gly-Pro.
Study Information
pubmed
2013
10.1134/s1068162013030151