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DSIP

Emideltide, DSIP nonapeptide, Delta sleep-inducing peptide

Quick Stats
Studies 458
Trials 82
Overview Studies Clinical Trials
Score 2
1984 pubmed

Evidence for peptide aggregation.

Kastin. A J AJ; Castellanos. P F PF; Fischman. A J AJ; Proffitt. J K JK; Graf. M V MV

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Key Findings

  • DSIP appears in multiple forms in serum, including a protein‑bound version and smaller fragments.
  • Adding acid or a metal‑chelator reduces some of the smaller‑size forms, indicating metal (especially iron) involvement.
  • Most of the detected forms still react with a DSIP‑specific antibody, meaning the peptide remains intact in those forms.

Practical Outcomes

  • For DIY users, this suggests DSIP’s activity could vary depending on how it’s prepared and whether it contacts metals or proteins in the body. Formulating DSIP with chelators or avoiding iron‑rich environments might improve consistency, but more research is needed before changing dosing protocols.

Summary

The study shows that the sleep‑related peptide DSIP can stick together, bind to proteins in blood, and interact with iron, creating several different forms when it’s mixed with serum.

Abstract

Evidence is presented that peptides may occur in aggregated form. Addition of 125I-Tyr-DSIP to serum resulted in four peaks after gel filtration chromatography on a column of Sephadex G-25. One of the peaks (C) eluted at the same position as the labeled peptide standard. Two Peaks (A and B) eluted before the standard and one (peak D) afterwards. The first peak (A) eluted at void volume, a position expected for labeled peptide bound to protein. The other two peaks (B and D), corresponding to smaller molecular size material, were greatly reduced by addition of glacial acetic acid or the chelating agent 1,10-phenanthroline before or even after mixing of the peptide with serum. Iron was one of the ions found to interact with 125I-Tyr-DSIP, and chromatography of a mixture of ferric chloride and peptide without serum resulted in the additional formation of peak B. A substantial portion of peaks A, B, and C (but not D) reacted with a specific DSIP antibody, indicating the presence of intact peptide. The results are consistent with the concept that peptides may occur in multiple forms.

Study Information

Provider

pubmed

Year

1984

DOI

10.1016/s0091-3057(84)80082-9