Research Peptide · For laboratory research use only
Also known as GRF 1-29 NH2, hGHRH(1-29)NH2, Sermorelin acetate
Sermorelin (GRF 1-29 NH2, also catalogued as hGHRH(1-29)NH2) is the synthetic, C-terminally amidated 1-29 fragment of human growth hormone-releasing factor (GRF, also GHRH). Full-length GRF was isolated in 1982 as a 44-residue peptide from a human pancreatic tumour, and its synthetic replicate stimulated growth hormone secretion in vitro and in vivo1.
Truncation studies in cultured rat anterior pituitary cells showed that the 1-29 amide retains full intrinsic activity at about half the potency of the full-length peptide2. Published work covers structure-activity studies in pituitary cells and animals, plasma degradation, a 1999 review of its clinical pharmacology, and anti-doping detection methods2,3,4,5,6.
As described in the research literature
As described in the research literature, sermorelin acts on the GRF receptor of the anterior pituitary to stimulate growth hormone secretion, and has been described as the shortest synthetic peptide with the full biological activity of GHRH5. In a series of C-terminally deleted analogues tested on rat anterior pituitary cells in monolayer culture, bioactivity fell gradually down to hGRF(1-34) and then held at about 50% of full-length GRF for the (1-31), (1-30) and (1-29) amides2.
Its short duration of action has been linked to rapid N-terminal cleavage. Incubation of GRF(1-44)-NH2 with human plasma produced GRF(3-44)-NH2, a fragment with less than one thousandth of the parent's biological activity, consistent with a plasma dipeptidylaminopeptidase4. The corresponding sermorelin fragment, GHRH(3-29), was identified as a metabolite during the development of a plasma detection method6. Substitution at position 2 was examined early: in rats, [D-Ala2]-GRF(1-29)-NH2 was reported to be about 50 times more potent than the parent 1-29 amide3.
What published studies have examined
The 44-residue GRF was isolated and sequenced from a human pancreatic tumour, and the synthetic peptide was tested for growth hormone release in vitro and in vivo1. C-terminally deleted analogues were then compared in rat anterior pituitary cell culture to define the minimal active core2, and position 1, 2 and 3 substituted analogues of GRF(1-29)-NH2 were compared for growth hormone secretion in rats and pigs3.
Degradation of GRF in plasma was characterised by HPLC, radioimmunoassay and bioassay, identifying cleavage between residues 2 and 3 as the main inactivating step4. In rat studies of GHRH analogues, intact sermorelin and related analogues were detected in plasma for at least 4 hours in a method development study6.
A 1999 review summarised the use of sermorelin as a provocative test of pituitary growth hormone reserve and its examination in paediatric clinical studies5. It is noted here for context on the compound's history, not as a description of effects.
Sources [5]
An immunoaffinity purification and nano-LC high resolution mass spectrometry method was developed and validated for sermorelin, CJC-1293, CJC-1295 and tesamorelin and their metabolites in plasma, with stability and metabolism examined in vitro and in rats6.
Sources [6]
Growth hormone-releasing factor from a human pancreatic tumor that caused acromegaly.
Guillemin R, Brazeau P, Böhlen P, et al. Science, 1982.
Synthesis and in vitro bioactivity of C-terminal deleted analogs of human growth hormone-releasing factor.
Ling N, Baird A, Wehrenberg WB, et al. Biochemical and Biophysical Research Communications, 1984.
Super-active analogs of growth hormone-releasing factor (1-29)-amide.
Lance VA, Murphy WA, Sueiras-Diaz J, et al. Biochemical and Biophysical Research Communications, 1984.
Rapid enzymatic degradation of growth hormone-releasing hormone by plasma in vitro and in vivo to a biologically inactive product cleaved at the NH2 terminus.
Frohman LA, Downs TR, Williams TC, et al. The Journal of Clinical Investigation, 1986.
Sermorelin: a review of its use in the diagnosis and treatment of children with idiopathic growth hormone deficiency.
Prakash A, Goa KL BioDrugs, 1999.
Qualitative identification of growth hormone-releasing hormones in human plasma by means of immunoaffinity purification and LC-HRMS/MS.
Knoop A, Thomas A, Fichant E, et al. Analytical and Bioanalytical Chemistry, 2016.
This page is provided for research and educational reference only. It does not constitute medical advice, dosing guidance, or a recommendation for use. All compounds are strictly for laboratory and in-vitro research purposes.