GHRP-6
Growth Hormone Releasing Peptide-6, Growth hormone-releasing hexapeptide, His-D-Trp-Ala-Trp-D-Phe-Lys-NH2
Exploring side-chain diversity by submonomer solid-phase aza-peptide synthesis.
Sabatino. David D; Proulx. Caroline C; Klocek. Sophie S; Bourguet. Carine B CB; Boeglin. Damien D; Ong. Huy H; Lubell. William D WD
Key Findings
- A solid‑phase submonomer method can produce aza‑peptide analogues of GHRP‑6 with good yield and purity.
- Ten different aza‑GHRP‑6 analogues were synthesized and characterized.
- Analogue 7a adopts a beta‑turn structure and shows a ~1000‑fold increase in selectivity for the CD36 receptor compared to regular GHRP‑6.
Practical Outcomes
- For biohackers, this work shows that tweaking the side‑chains of GHRP‑6 can dramatically change which receptors it hits, hinting at the possibility of more targeted analogues. However, the paper does not provide dosing guidance, safety data, or direct performance benefits, so it’s not yet ready for real‑world use.
Summary
Scientists made a new, easier way to create modified versions of the peptide GHRP-6. One of these new versions (called 7a) folds into a shape that makes it bind a different receptor (CD36) a thousand times better than the original peptide. The study is mostly about chemistry, not about how to use the peptide in humans.
Abstract
Submonomer synthesis of aza-peptides featuring regioselective alkylation of peptide-bound aza-Gly residues provided ten aza-analogues of the Growth Hormone Releasing Peptide-6 (GHRP-6) in 15-42% yield and purity generally >or=90%. Circular dichroism demonstrated that azaPhe-peptide 7a induced a beta-turn conformation which may be responsible for its 1000-fold improvement in GHRP-6 selectivity for the CD36 receptor. This versatile method for making aza-peptides avoids solution-phase hydrazine synthesis and is well suited for studying side-chain-activity relationships of biologically active peptides.
Study Information
pubmed
2009
2009-08-20T00:00:00.000Z
10.1021/ol901423c
66