What is the Origin of Modified GRF 1-29?

The peptide's structure is derived from the native human GHRH, which was originally isolated from a pancreatic tumor. The "Modified" descriptor refers to strategic amino acid substitutions, specifically to resist rapid enzymatic cleavage by the plasma protease Dipeptidyl Peptidase-IV (DPP-IV). This critical modification was engineered to improve the pharmacological profile, allowing for a more clinically useful and sustained action.

What is the Mechanism of Modified GRF 1-29?

Modified GRF 1-29 acts as a highly selective agonist, binding to the Growth Hormone-Releasing Hormone Receptor (GHRH-R) expressed on the somatotroph cells in the anterior pituitary. Its binding stimulates the synthesis and release of GH in a manner that closely mimics the body's natural, physiological pulsatile rhythm. By acting upstream, it maintains the integrity of the hypothalamic-pituitary axis and avoids the potential negative feedback associated with direct, continuous administration of exogenous GH.

Modified GRF 1-29

Meaning

Modified GRF 1-29, which is also clinically known as Sermorelin, is a synthetic peptide analog encompassing the first 29 amino acids of the naturally occurring Growth Hormone-Releasing Hormone (GHRH) sequence. This therapeutic peptide is characterized by specific chemical modifications that dramatically enhance its metabolic stability and prolong its half-life in the systemic circulation compared to the native hormone. It is utilized clinically as a potent secretagogue to stimulate the pituitary gland’s pulsatile release of endogenous Growth Hormone (GH).