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DSIP

Emideltide, DSIP nonapeptide, Delta sleep-inducing peptide

Quick Stats
Studies 458
Trials 82
Score 2
1988 pubmed

Enzymatic synthesis of delta sleep-inducing peptide.

Sakina. K K; Kawazura. K K; Morihara. K K

Key Findings

  • DSIP can be assembled enzymatically from three tripeptide fragments using papain or alpha‑chymotrypsin.
  • Adding N‑alpha‑protected amino acids or peptide esters and using alkaline pH prevents secondary hydrolysis during synthesis.
  • The enzymatically produced DSIP is chemically identical to DSIP made by conventional synthetic routes.

Practical Outcomes

  • The study shows a viable enzymatic route to produce DSIP, which could interest those wanting a non‑chemical synthesis path, but it requires specialized enzymes, protected amino acids, and chromatography equipment. For most biohackers, the method isn’t a ready‑to‑use protocol, though it confirms that DSIP made this way is comparable to standard versions.

Summary

Scientists figured out a way to build the sleep‑helping peptide DSIP using enzymes instead of traditional chemistry. The process uses papain or chymotrypsin to link three short peptide pieces, adds protective groups to stop unwanted reactions, and finishes with purification. The final product looks the same as chemically made DSIP, but the method is more complex than a typical DIY recipe.

Abstract

The delta sleep-inducing peptide was assembled enzymatically from three tripeptide fragments. All the peptide bonds were prepared by either papain- or alpha-chymotrypsin-mediated synthesis. Secondary hydrolysis was suppressed by introducing N alpha-protected amino acid or peptide esters as carboxyl components and using an alkaline pH. The protected nonapeptide was oxidized with ferric chloride to deprotect the C-terminal phenylhydrazide and then hydrogenated. The homogeneous peptide was obtained by reversed phase high-performance liquid chromatography. Comparison of enzymatic and chemical preparations showed no obvious differences.

Study Information

Provider

pubmed

Year

1988

DOI

10.1111/j.1399-3011.1988.tb00030.x