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13

Sermorelin

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All information below is drawn from preclinical research literature and is provided for educational and informational purposes only. It does not constitute medical advice, imply therapeutic outcomes, or endorse any specific application.

Chemical Identification

Property

Value

CAS Number86168-78-7
PubChem CID16132413 / 16129620
SequenceHuman GRF 1-29 Amide
Molecular FormulaC149H246N44O42S
Molecular Weight3357.9 Da

Reference Studies

[1]https://pubmed.ncbi.nlm.nih.gov/18046908/[2]https://www.invivochem.com/grf-1-29-amide-human.html

Overview

General Research Context

Sermorelin is a synthetic truncation of endogenous Growth Hormone-Releasing Hormone, consisting of the first 29 amino acids (GRF 1-29) of the 44-amino acid native hormone. In laboratory research, it has been studied to examine GHRH receptor binding kinetics and somatotroph cell signaling pathways.

Published analytical work has established that the receptor-binding domain of GHRH is contained within its N-terminal 29 residues, forming the basis for Sermorelin as a research tool in neuroendocrine studies.

Areas of Investigation

Observed Interactions and Background

Analytical studies established that the receptor-binding activity of the 44-amino acid GHRH is contained within its N-terminal 29 amino acids. Sermorelin was designed to retain the receptor-binding domain while simplifying laboratory synthesis.

In preclinical cellular assays, Sermorelin has been observed to bind the GHRH receptor and engage the cAMP second messenger system in isolated somatotroph preparations. Due to the absence of protective structural modifications, the compound possesses a short plasma half-life in physiological systems (often under 15 minutes in animal models). These observations are derived from preclinical research settings.

Laboratory Notes

Synthesis and Stability Notes

Sermorelin is synthesized via standard stepwise SPPS. Due to its sequence, it is highly susceptible to rapid deamidation and oxidative degradation at ambient temperatures in liquid environments. It must be maintained strictly as a lyophilized powder at -20°C. In the laboratory, RP-HPLC purification profiles must specifically and meticulously monitor for the presence of truncated failure sequences.

Disclaimer: All information provided herein is strictly for educational and laboratory research reference purposes only. Saga does not endorse, interpret, or evaluate these preclinical studies for any specific in vivo application or human therapeutic outcome.

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