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Humanin

HN, S14G-Humanin

Quick Stats
Studies 491
Trials 100
Score 3
2004 pubmed 11 citations

High-yield, solid-phase synthesis of humanin, an Alzheimer's disease associated, novel 24-mer peptide which contains a difficult sequence.

Evangelou. Alexandra A; Zikos. Christos C; Livaniou. Evangelia E; Evangelatos. Gregory P GP

Key Findings

  • Humanin can be produced by Fmoc solid‑phase synthesis on a 2‑Cl‑tritylamidomethyl polystyrene resin
  • The segment R4G5F6S7C8L9 is a ‘difficult sequence’ that requires longer deprotection steps
  • The optimized protocol yields a high overall amount of pure humanin

Practical Outcomes

  • If you have chemistry skills and the right equipment, you can synthesize humanin yourself instead of buying it, giving you more control over purity and supply. However, the process is still technically demanding and not a simple at‑home hack.

Summary

Scientists figured out a reliable way to make the 24‑amino‑acid peptide humanin in the lab using solid‑phase chemistry, even though part of its sequence is tricky to handle. This method gives a good amount of pure peptide, which is needed for any further testing or use.

Abstract

Humanin is a novel, 24-mer residue bioactive peptide, which antagonizes Alzheimer's disease (AD) related neurotoxicity and offers a hope for developing new therapeutics against AD. Access to adequate amounts of pure humanin is a prerequisite for further, thorough, investigation of the pharmacological properties and therapeutic potency of the peptide. Until now, humanin has been obtained mainly by molecular biology techniques. In this work the Fmoc solid-phase synthesis of humanin on an in-house prepared 2-Cl-tritylamidomethyl polystyrene resin is described fully. Special precautions, i.e. prolonged deprotection steps, should be taken to achieve a high overall yield, since humanin seems to contain a 'difficult sequence' (R4G5F6S7C8L9) near its highly lipophilic, biologically important region L9L10L11L12.

Study Information

Provider

pubmed

Year

2004

Date

2004-10-01T00:00:00.000Z

DOI

10.1002/psc.572

Citations

11

References

21