Potent trypsin-resistant hGH-RH analogues.
Izdebski. Jan J; Witkowska. Ewa E; Kunce. Danuta D; Orłowska. Alicja A; Baranowska. Bogusława B; Wolińska-Witort. Ewa E
Key Findings
- Three new GHRH analogues were engineered to resist trypsin digestion.
- The analogues showed roughly 50‑fold higher potency than native hGH‑RH‑(1‑29) when injected subcutaneously in rats.
- The peptides are being considered for future clinical use in growth‑hormone deficiency therapy.
Practical Outcomes
- For biohackers, the study signals that more stable and potent GHRH‑based peptides are under development, which could eventually lead to stronger, longer‑lasting GH‑releasing supplements. However, because the data are limited to animal models, there are no immediate dosage or protocol recommendations for human use.
Summary
Researchers made new versions of the growth‑hormone‑releasing hormone (GHRH) that are much harder for the body to break down and work about 50 times better than the original peptide in rats. These modified peptides could eventually be used to treat growth‑hormone deficiency, but they have only been tested in animals so far.
Abstract
A series of analogues of hGH-RH-(1-29)-NH2 designed to have metabolic stability has been synthesized. Standard Boc-SPPS was employed, modified to permit the guanidinylation of amino side-chains after chain assembly but before release from the resin. [Dat1, Har(11, 12, 20, 21, 29), Ala15, Nle27, Asp28]-, [Dat1, Har(11, 20, 29), Orn12, Ala15, Nle27, Asp28]-, and [Dat1, Gap(11,12, 21, 29), Ala15, Har20, Nle27, Asp28]-hGH-RH-(1-29)-NH2 were completely resistant to trypsin and about 50 times as potent as hGH-RH-(1-29)-NH2 itself when injected subcutaneously in rats. These peptides are candidates for clinical application in the therapy of GH deficiency.
Study Information
pubmed
2004
2004-08-01T00:00:00.000Z
10.1002/psc.563
7
13