Menu
Peptide Database
Results
No peptides found
Featured

Use search to browse all 100+ peptides

DSIP

Emideltide, DSIP nonapeptide, Delta sleep-inducing peptide

Quick Stats
Studies 458
Trials 82
Score 2
2006 pubmed

[Interaction of delta sleep-inducing peptide and its analogues with cellular membranes: a structure-function analysis].

Mikhaleva. I I II; Rikhireva. G T GT; Prudchenko. I A IA; Golubev. I N IN

Key Findings

  • Active DSIP and certain analogues cause a reliable disordering of lipids in platelet membranes, similar to natural DSIP.
  • An inactive hexapeptide analogue only caused a slight, nonspecific lipid disturbance.
  • The degree of membrane disorder correlates with the peptide’s biological activity in vivo, especially under stress conditions.

Practical Outcomes

  • For biohackers, the main takeaway is that DSIP’s benefits may stem from its interaction with cell membranes, suggesting that formulations that enhance membrane penetration could be more effective. However, the paper does not provide specific dosing or protocol changes, so it serves more as a mechanistic insight than a direct actionable guide.

Summary

The study shows that delta sleep‑inducing peptide (DSIP) and its active analogues can disturb the structure of cell membranes, especially in platelets, and that this membrane‑disordering matches how well the peptides work in live animals. Inactive versions don’t cause the same effect. The researchers think DSIP’s ability to change membrane dynamics may be part of why it helps with stress and sleep.

Abstract

The possibility of a correlation between the membrane properties of the delta sleep-inducing peptide (DSIP) and its analogues and their biological activity in vivo was examined by a comparative study of the membrane effects of these peptides. The peptides exhibiting biological activity in vivo were shown to cause a statistically reliable disordering of lipids in thrombocyte plasma membranes similar to the effect of DSIP. The membrane effect of the D-Val2, D-Tyr2, and Tyr1, Pro2 analogues of DSIP had the same bimodal dose dependence characteristic of natural DSIP. Only a slight nonspecific lipid disordering was registered for Trp-Asp-Ala-Ser-Gly-Glu, a biologically inactive hexapeptide analogue. These results indicate a correlation between the biological activity of the peptides during in vivo tests and their membrane properties in vitro. The structure-function relationship was studied within the group of DSIP analogues examined in vitro. The DSIP modeling effect, especially pronounced under the action of stress factors, was suggested to be directly associated with the ability of DSIP to change the dynamic structure of biological membranes.

Study Information

Provider

pubmed

Year

2006

DOI

10.1134/s1068162006020087