[Leu-enkephalin homogeneously labeled with tritium in studying the Selank inhibiting effect on the enkephalin-degrading enzymes of human plasma].
Zolotarev. Iu A IuA; Sokolov. O Iu OIu; Kost. N V NV; Vas'kovskiĭ. B V BV; Miasoedov. N F NF; Zozulia. A A AA
Key Findings
- Selank selectively inhibits carboxypeptidases and dicarboxypeptidases that degrade Leu‑enkephalin
- In plasma, about 80% of enkephalin breakdown is due to aminopeptidases, with smaller roles for dipeptidyl‑ and carboxypeptidases
- A new carboxypeptidase‑mediated degradation pathway for Leu‑enkephalin was identified
Practical Outcomes
- Selank may modestly increase endogenous enkephalin levels by slowing their breakdown, potentially supporting stress resilience or mild analgesia. However, the evidence is limited to in‑vitro enzyme assays, so no concrete dosing or protocol recommendations can be drawn from this paper.
Summary
The study shows that Selank, a peptide some people use for mood and stress, can block certain enzymes (carboxypeptidases) that break down the natural pain‑relief molecule Leu‑enkephalin in blood plasma. This suggests Selank might help keep enkephalins around longer, but the work was done in a test‑tube setting, not in people, and it doesn’t tell you how much to take or what effects to expect.
Abstract
A method of analysis of enkephalinase activity in blood plasma based on the application of Leu-enkephalin generally labeled with tritium at all its amino acid residues was developed. The method allows the simultaneous estimation of activity of several peptidases in microquantities of tissues. [G-3H]Leu-enkephalin was prepared by the method of solid phase catalytic isotope exchange (120 Ci/mmol) and subjected to proteolysis by the treatment with blood plasma. The resulting radioactive metabolites were separated by HPLC in the presence of the mixture of unlabeled fragments of Leu-enkephalin as internal standards. It was shown that aminopeptidases, dipeptidylaminopeptidases, and dipeptidylcarboxypeptidases respond for approximately 80%, 2%, and 10% of the total enzymatic activity, respectively. The new pathway of degradation of Leu-enkephalin by carboxypeptidase that provides for approximately 6% of the total enkephalin-degrading activity was discovered. Bestatin was shown to predominantly inhibit aminopeptidases and carboxypeptidases, whereas Selank is more specific for carboxypeptidases and dicarboxypeptidases. The English version of the paper: Russian Journal of Bioorganic Chemistry, 2004, vol. 30, no. 3; see also http://www.maik.ru.
Study Information
pubmed
2004
10.1023/b:rubi.0000030126.09208.c3