GHRP-6
Growth Hormone Releasing Peptide-6, Growth hormone-releasing hexapeptide, His-D-Trp-Ala-Trp-D-Phe-Lys-NH2
Copper-catalyzed N-arylation of semicarbazones for the synthesis of aza-arylglycine-containing aza-peptides.
Proulx. Caroline C; Lubell. William D WD
Key Findings
- A copper‑catalyzed N‑arylation approach was used to create 13 aza‑arylglycine‑containing peptides based on the GHRP‑6 sequence.
- The method allowed incorporation of aza‑indolylglycine (aza‑Trp) and aza‑imidazoylglycine (aza‑His) residues via heteroaryl iodides.
- Circular dichroism showed that aza‑peptides with aza‑Trp at position 4 tend to form beta‑turn structures.
Practical Outcomes
- The study provides a synthetic route for creating GHRP‑6 analogs, which could be useful for drug‑design researchers, but it offers no direct guidance on dosing, safety, or performance effects for self‑experimenters. For the biohacker community, the findings are not actionable in everyday protocols.
Summary
Scientists described a new lab method to make modified versions of the GHRP‑6 peptide, but the work is focused on chemistry techniques and structural analysis, not on how the peptide works in the body or how to use it.
Abstract
Parallel synthesis of 13 aza-arylglycine peptides, based on the hexapeptide sequence of Growth Hormone Releasing Peptide-6 (GHRP-6), was accomplished via selective N-arylation of a semicarbazone peptide building block anchored on Rink amide resin. Aza-peptides possessing aza-indolylglycine and aza-imidazoylglycine residues were obtained through use of the corresponding heteroaryl iodides, yielding, respectively, aza-Trp and aza-His peptidomimics. CD spectroscopy indicated the propensity for aza-peptides, containing aza-arylglycines at the Trp(4) position of the GHRP-6 sequence, to adopt beta-turns.
Study Information
pubmed
2010
2010-07-02T00:00:00.000Z
10.1021/ol100932m
21