Everything below concerns GHRH analogue. We keep the language plain, cite what the science says, and separate well-supported claims from open questions.
Last reviewed on 2026-02-23. Where a claim depends on a specific study, the study is described rather than over-claimed.
Tesamorelin is a synthetic peptide that belongs to the growth hormone-releasing hormone (GHRH) family. Its sequence corresponds to the fully active 44-amino-acid form of human GHRH, with a single structural modification: the addition of a trans-3-hexenoyl group at the N-terminus. That modification is not found in the naturally occurring hormone and was introduced deliberately during development to improve stability against enzymatic degradation. The compound is therefore best described as a stabilized analogue rather than a naturally occurring peptide.
The native hormone is produced in the hypothalamus and acts on the anterior pituitary. Binding of GHRH to its receptor stimulates synthesis and release of growth hormone into circulation. Because the analogue retains the receptor-binding region of the parent sequence, it engages the same receptor and triggers the same downstream signaling. The result is increased growth hormone secretion from pituitary cells, which in turn influences hepatic production of insulin-like growth factor 1. This axis is the basis for the compound's measured biological effects.
Tesamorelin is a synthetic analog of growth hormone-releasing hormone, a peptide hormone produced by the hypothalamus. The molecule retains the 44-amino-acid sequence of human GHRH and carries a trans-3-hexenoyl modification at its N-terminus. This modification increases resistance to enzymatic degradation and extends the peptide's functional stability relative to native GHRH. The compound is supplied as a lyophilized powder for reconstitution and subcutaneous administration in clinical settings. Its development code was TH9507, and it belongs to the GHRH analog class. It is not a growth hormone product; instead, it acts upstream to stimulate endogenous growth hormone release.
Clinical interest in tesamorelin arose from the need to address visceral adiposity in people living with HIV. Antiretroviral therapy improved survival but was associated in some patients with central fat accumulation, altered lipid profiles, and metabolic complications. This condition, often called HIV-associated lipodystrophy, involves excess visceral adipose tissue that is difficult to manage through diet and exercise alone. Investigators evaluated tesamorelin because GHRH analogs can stimulate growth hormone secretion and influence fat distribution without direct liposuction or invasive procedures.
A Phase 3 program led to regulatory approval in the United States in 2010 for reduction of excess visceral abdominal fat in adults with HIV and lipodystrophy. Subsequent studies examined effects on liver fat, muscle area, and metabolic markers, with mixed findings for some endpoints. Long-term cardiovascular outcomes and effects on mortality remain uncertain because most trials were relatively short and focused on imaging-based fat measurements. Use in populations without HIV has been studied experimentally but is not part of the approved indication.
| Property | Value | Notes |
|---|---|---|
| Molecular formula | C221H366N72O67S | Reflects a 44-residue peptide with one N-terminal modification |
| Approximate molecular weight | 5136 Da | Sequence length and single acyl group determine the mass |
| Appearance | White to off-white lyophilized powder | Typical form of a purified synthetic peptide |
| Solubility class | Soluble in water and aqueous buffer | Peptide backbone favors aqueous dissolution |
| Common synonyms | GHRH(1-44) analogue; Egrifta | Descriptive name and approved brand name |
Tesamorelin is a synthetic peptide analog of growth hormone-releasing hormone, composed of 44 amino acids. It was designed to retain the biological activity of the native hormone while resisting rapid enzymatic degradation. The compound is classified as a growth hormone secretagogue and belongs to the broader family of hypothalamic releasing factors. In research and clinical settings, it is studied for its ability to stimulate pituitary growth hormone release. Its structure includes a modification at the N-terminus that contributes to an extended half-life relative to native growth hormone-releasing hormone.
Tesamorelin binds to growth hormone-releasing hormone receptors on the surface of pituitary somatotroph cells. This binding activates adenylate cyclase, raising intracellular cyclic AMP levels and triggering the release of growth hormone into circulation. The elevated growth hormone then stimulates hepatic production of insulin-like growth factor 1. Because the effect is mediated through the endogenous axis, secretion remains subject to feedback regulation. This distinguishes it from direct growth hormone administration, which bypasses pituitary control entirely.
Tesamorelin is a synthetic peptide analog of growth hormone-releasing hormone, built from 44 amino acids. Its sequence follows the natural human GHRH(1-44) backbone, with a trans-3-hexenoyl group attached to the N-terminal tyrosine. This modification blocks recognition by dipeptidyl peptidase IV, the enzyme that rapidly truncates the native hormone in circulation. The result is a molecule with a substantially longer plasma residence time than unmodified GHRH, which makes it practical for clinical and laboratory study.
Receptor-level activity begins when the peptide binds the GHRH receptor, a class B G-protein-coupled receptor found on pituitary somatotroph cells. Occupancy triggers Gs-mediated activation of adenylyl cyclase and a rise in intracellular cyclic AMP, which in turn promotes synthesis and pulsatile release of growth hormone. Because the compound acts upstream of the growth hormone axis rather than supplying hormone directly, its effect depends on intact pituitary function. Binding studies in cell culture and animal models have established this pathway; the detailed kinetics of receptor recycling in humans remain less well characterized.
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Nobel physics laureate Steven Weinberg said that the Nobel committee "fleeced" Dyson, but Dyson remarked in 2009, "I think it's almost true without exception if you want to win a Nobel Prize, you should have a long attention span, get hold of some deep and important problem and stay with it for ten years. That wasn't my style." Dyson was a regular contributor to The New York Review of Books, and published a memoir, Maker of Patterns: An Autobiography Through Letters in 2018. In 2012 Dyson published (with William H. Press) a fundamental new result about the prisoner's dilemma in the Proceedings of the National Academy of Sciences of the United States of America.
===== MeSH D08.811.682.662 – oxidoreductases acting on ch-nh group donors ===== MeSH D08.811.682.662.162 – dihydropteridine reductase MeSH D08.811.682.662.171 – FMN reductase MeSH D08.811.682.662.217 – methylenetetrahydrofolate dehydrogenase (nad+) MeSH D08.811.682.662.253 – methylenetetrahydrofolate dehydrogenase (nadp) MeSH D08.811.682.662.290 – methylenetetrahydrofolate reductase (nadph2) MeSH D08.811.682.662.582 – oxidoreductases, n-demethylating MeSH D08.811.682.662.582.276 – aminopyrine n-demethylase MeSH D08.811.682.662.582.338 – cytochrome p-450 cyp2e1 MeSH D08.811.682.662.582.353 – cytochrome p-450 cyp3a MeSH D08.811.682.662.582.361 – dihydropteridine reductase MeSH D08.811.682.662.582.369 – dimethylglycine dehydrogenase MeSH D08.811.682.662.582.400 – ethylmorphine-n-demethylase MeSH D08.811.682.662.582.550 – sarcosine dehydrogenase MeSH D08.811.682.662.582.700 – sarcosine oxidase MeSH D08.811.682.662.640 – proline oxidase MeSH D08.811.682.662.680 – pyridoxamine-phosphate oxidase MeSH D08.811.682.662.693 – 1-pyrroline-5-carboxylate dehydrogenase MeSH D08.811.682.662.695 – pyrroline carboxylate reductases MeSH D08.811.682.662.750 – saccharopine dehydrogenases MeSH D08.811.682.662.825 – tetrahydrofolate dehydrogenase
Sources: en.wikipedia.org
In the mid-2010s, Valve began experimenting with virtual reality (VR). They built prototypes using their various intellectual properties such as Portal, and found that Half-Life best suited VR. Their flagship VR game, Half-Life: Alyx, entered production using Valve's new Source 2 engine in 2016, with the largest team in Valve's history, including members of Campo Santo, a studio Valve acquired in 2018.
==== Brand names of valproate semisodium ==== Brazil – Depakote by Abbott Laboratories and Torval CR by Torrent do Brasil Canada – Epival by Abbott Laboratories Mexico – Epival and Epival ER (extended release) by Abbott Laboratories United Kingdom – Depakote (for psychiatric conditions) and Epilim (for epilepsy) by Sanofi-Aventis and generics United States – Depakote and Depakote ER (extended release) by Abbott Laboratories and generics India – Valance and Valance OD by Abbott Healthcare Pvt Ltd, Divalid ER by Linux laboratories Pvt Ltd, Valex ER by Sigmund Promedica, Dicorate by Sun Pharma Germany – Ergenyl Chrono by Sanofi-Aventis and generics Chile – Valcote and Valcote ER by Abbott Laboratories France and other European countries – Depakote Peru – Divalprax by AC Farma Laboratories China – Diprate OD
The genome of a given organism contains thousands of genes, but not all these genes need to be active at any given moment. A gene is expressed when it is being transcribed into mRNA and there exist many cellular methods of controlling the expression of genes such that proteins are produced only when needed by the cell. Transcription factors are regulatory proteins that bind to DNA, either promoting or inhibiting the transcription of a gene. Within the genome of Escherichia coli bacteria, for example, there exists a series of genes necessary for the synthesis of the amino acid tryptophan. However, when tryptophan is already available to the cell, these genes for tryptophan synthesis are no longer needed. The presence of tryptophan directly affects the activity of the genes—tryptophan molecules bind to the tryptophan repressor (a transcription factor), changing the repressor's structure such that the repressor binds to the genes. The tryptophan repressor blocks the transcription and expression of the genes, thereby creating negative feedback regulation of the tryptophan synthesis process.
Sources: en.wikipedia.org
It shares the 44-residue sequence of human GHRH but carries an added trans-3-hexenoyl group at its N-terminus. That addition does not occur in the natural hormone and serves mainly to resist enzymatic breakdown. The receptor target and signaling pathway remain the same.
It binds the growth hormone-releasing hormone receptor on anterior pituitary cells. Activation of that receptor promotes synthesis and release of growth hormone. The effect propagates through the growth hormone and insulin-like growth factor 1 axis.
Native GHRH is cleared quickly by peptidases, which limits how long it can stimulate its receptor. The added group hinders one of the primary cleavage enzymes. The practical consequence is a longer period of receptor activity per dose.
It is a synthetic peptide analog of human growth hormone-releasing hormone. It is used clinically to reduce excess visceral abdominal fat in adults with HIV-associated lipodystrophy. It works by stimulating pituitary growth hormone release.