Tesamorelin - Frequently Asked Questions

Tesamorelin is a synthetic growth hormone-releasing hormone (GHRH/GRF) analog. The entry describes it as an N-terminally lipid-modified 44-residue peptide and a GHRH receptor (GHRHR) agonist, meaning it is built on the native GHRH scaffold with a stabilizing structural modification.

Its molecular target is the growth hormone-releasing hormone receptor (GHRHR), a class B G-protein-coupled receptor expressed on anterior pituitary somatotroph cells. In receptor-level and cell-based systems, tesamorelin acts as a GHRHR agonist.

Per the record, receptor engagement couples to the stimulatory G-protein (Gs), activating adenylyl cyclase and raising intracellular cAMP, which activates protein kinase A (PKA). PKA phosphorylates transcription factors such as CREB, modulating growth-hormone gene transcription and somatotroph secretory-vesicle mobilization, the canonical GHRH signaling cascade.

It is the full native human GHRH(1-44) sequence, one-letter YADAIFTNSYRKVLGQLSARKLLQDIMSRQQGESNQERGARARL, bearing a trans-3-hexenoyl group on the alpha-amino group of N-terminal Tyr1 and a C-terminal amide (-NH2).

The average molecular weight is 5135.9 g/mol (approximately 5136 Da), and the molecular formula is C221H366N72O67S, both attributed to PubChem CID 16137828 computed properties. The molecular weight is the value used for molar-concentration calculations.

The CAS Registry Number for the free base is 218949-48-5. The PubChem Compound Identifier (CID) is 16137828, and the original development code was TH9507 (TH-9507), recorded from the Falutz et al. 2010 pooled phase 3 analysis.

The N-terminal trans-3-hexenoyl acylation on Tyr1 confers resistance to dipeptidyl peptidase-4 (DPP-4) cleavage, which is the principal route of native GHRH inactivation. This prolongs the molecule's stability while preserving its receptor-binding determinants.

Listed areas include GHRHR class B GPCR binding and agonist pharmacology; Gs/adenylyl cyclase/cAMP/PKA signal-transduction studies in somatotroph cell models; CREB phosphorylation and growth-hormone gene transcription; DPP-4 enzymatic-stability and degradation kinetics of N-acylated GHRH analogs; structure-activity relationships of N-terminal lipidation; and population/preclinical pharmacokinetic modeling of long-acting GHRH analogs.

No numeric half-life is provided in the record. The entry supports a degradation-resistance mechanism (N-terminal acylation blocking DPP-4 cleavage to prolong stability) but does not state quantitative pharmacokinetic values, so none should be inferred from this data alone.

It is supplied lyophilized and reconstituted for research handling by dissolving a known peptide mass in bacteriostatic water to a calculated concentration, using the 5135.9 g/mol molecular weight for molar conversions. As a peptide-class principle, lyophilized solid is stored frozen and reconstituted stock refrigerated and protected from light, with minimal freeze-thaw.

No. This is a research-use-only reference. All framing is in-vitro, receptor-signaling, and laboratory-research oriented; reconstitution and handling describe laboratory preparation for in-vitro work, not any human dosing or administration protocol.

The cited sources are Falutz et al. 2010 (JCEM pooled phase 3 analysis), Tomlinson 2006 (Current Opinion in Investigational Drugs drug evaluation), Dhillon 2011 (Drugs review), Stanley et al. 2014 (JAMA randomized clinical trial), and Gonzalez-Sales et al. 2015 (Clinical Pharmacokinetics population pharmacokinetic analysis).