Tesamorelin

Tesamorelin in brief

Tesamorelin (development code TH9507) is a synthetic analogue of human growth hormone-releasing hormone: the full 44-residue amidated sequence with one added trans-3-hexenoyl chain on the N-terminal tyrosine (C221H366N72O67S, about 5136 g/mol). That acyl group sits where dipeptidyl peptidase IV cuts the natural hormone, and a 2007 non-clinical report described the analogue as resistant to that enzyme and slower to degrade in plasma. A 412-participant randomised placebo-controlled trial showed it engages the growth hormone axis in people. Its defining chemical property rests on that one report, and no receptor affinity figure, cell study or 3D structure of the molecule was found.^{[1,2,3,4,5,6]}

Tesamorelin regulatory status

Tesamorelin is approved in the United States for the reduction of excess abdominal fat in HIV-infected adults with lipodystrophy, with an initial US approval in 2010. In the EU the marketing authorisation application for the same indication was withdrawn by the applicant in 2012, and the Health Canada Drug Product Database lists the one product that reached the Canadian market as cancelled post market since 2022 (both searched November 2026). The 2026 WADA Prohibited List names tesamorelin under S2.2.4, growth hormone releasing factors (GHRH and its analogues), in the class prohibited at all times. It does not appear on the FDA's list of bulk drug substances that may present significant safety risks, in either the category 2 table or the table of nominations withdrawn by their nominators (page content current as of 22 April 2026), which is what would be expected for a substance that holds an approval.^{[7,8,9,10,11,12]}

Tesamorelin at a glance

• One covalent change from a natural human hormone. The chain is the mature 44-residue growth hormone-releasing hormone sequence, amide and all, with (3E)-hex-3-enoyl on the Tyr1 amine. The whole molecule is C221H366N72O67S, about 5136 g/mol, 5132.7166 Da monoisotopic.^[1,2,13]
• This is an approved prescription medicine, which is the context for its whole clinical literature. The FDA approved it in 2010 for the reduction of excess abdominal fat in adults with HIV-associated lipodystrophy; the European application for the same indication was withdrawn by the applicant in 2012, and the one Canadian product is recorded as cancelled post market. It is prohibited in sport at all times under WADA class S2.2.4 as a growth hormone releasing factor. Researchers reach for it because it is the full natural hormone sequence with a single designed change, which makes it the cleanest available probe of what that one change does.^{[7,8,9,10,11]}
• The acyl group sits where a protease cuts. Plasma degradation of the natural hormone begins with a single dipeptidyl peptidase IV cleavage of the Ala2-Asp3 bond, and work on the analogue series showed that blocking or reconfiguring the N-terminal amine abolishes that cleavage outright. The 2007 non-clinical report describes the hexenoyl analogue as resistant to that enzyme and as degrading more slowly in rat, dog and human plasma than the unmodified hormone.^[4,14,3]
• There is no published affinity or potency figure for this molecule at its receptor. No Kd, Ki or EC50 for the acylated peptide was found in any indexed source, and no study compares it with the unmodified hormone in a binding or cAMP assay, so the receptor half of its design is uncharacterised. Why there is also no structure to show is set out in the molecular structure section.^[6,15,16,1]
• The molecular-level evidence specific to the compound is mostly analytical and transcriptomic rather than receptor-level: four independent mass-spectrometry methods identify it in urine or plasma down to the picogram per millilitre range, and two studies on paired human liver specimens report changes in hepatic gene sets and in three named plasma proteins.^{[17,18,19,20,21,22,23]}

What is Tesamorelin?

Tesamorelin is a synthetic analogue of growth hormone-releasing hormone, the 44-residue hypothalamic peptide also called somatoliberin. The natural hormone is cut out of a 108-residue precursor as residues 32 to 75 and is amidated on its C-terminal leucine; its receptor is a class B1 G protein-coupled receptor on pituitary somatotropes that couples to the stimulatory G protein Gs. Class B1 is the peptide-hormone branch of that receptor family, distinguished by a large extracellular domain that catches the peptide's far end before the rest of it reaches into the membrane-spanning bundle. Tesamorelin reproduces that sequence exactly and adds one thing to it, a six-carbon acyl chain on the amine of the first residue.^[13,24,2,25]

That single change is the whole design, and it was aimed at a known chemical liability rather than at the receptor. The hormone's N-terminus is the substrate of dipeptidyl peptidase IV, a serum and cell-surface enzyme that clips two residues at a time off the front of a peptide and which removes the first two residues of this one in a single step. The 2007 non-clinical report describes the molecule as hGRF(1-44)NH2 minimally modified by addition of a trans-3-hexenoyl moiety to Tyr1 and reports that it resists that enzyme, degrades more slowly in rat, dog and human plasma than the unmodified hormone, and shows a longer plasma elimination profile in animals.^[3,4]

Two sets of facts place the clinical literature below, and both come from the regulator's own record. On status: the FDA approved the molecule in 2010 for the reduction of excess abdominal fat in adults with HIV-associated lipodystrophy, the European marketing authorisation application for the same indication was withdrawn by the applicant in 2012, and the Health Canada product database records the one Canadian product as cancelled post market since 2022. On measurable properties: the current prescribing information gives a mean elimination half-life of 11 minutes in healthy subjects and a mean volume of distribution of 4.8 plus or minus 1.9 litres per kilogram, and states in terms that no formal metabolism studies have been performed in humans. A population model fitted to a phase I dataset puts plasma clearance at 1,060 litres per hour with 33.6 percent interindividual variability and volume of distribution at 200 litres. An 11 minute half-life is the number to hold on to when reading anything about this molecule: it is short, and the design that produced it was aimed at a protease rather than at duration.^{[7,8,9,10,26]}

It reached the literature through a 412-participant randomised placebo-controlled trial published in 2007, in which circulating insulin-like growth factor 1, the liver-made peptide whose level is the standard downstream readout of growth hormone secretion, rose by 81 percent against a 5 percent fall on placebo, which is the measurement establishing that the molecule engages the growth hormone axis in people. Later work built on tissue collected in a 2019 trial. The clinical record is cited here bibliographically; this page reproduces no dose, no regimen and no clinical endpoint.^[5,27]

The controlled trials reported harms as well as readouts, and they are recorded here with their figures because the regulator's label is the one place they are counted. Across the clinical programme 740 participants received the compound, 543 of them in the 26-week placebo-controlled phase against 263 on placebo. The categories the label names as most common are hypersensitivity reactions such as rash and urticaria, fluid-retention reactions such as joint pain, pain in an extremity, peripheral oedema and carpal tunnel syndrome, raised blood glucose, and local reactions at the site where the medicine was given, which was the most frequent single category at 17 percent against 6 percent on placebo. Joint pain ran 13 against 11 percent. The finding that matters most is metabolic: against a mean baseline HbA1c of 5.3 percent in both groups, participants on the compound had an increased risk of reaching an HbA1c of 6.5 percent or above, 5 percent against 1 percent, with a hazard ratio of 3.3 and a 95 percent confidence interval of 1.4 to 9.6. That is a measured harm in the population studied, and it is the counterpart of the growth hormone axis engagement that the 81 percent rise in insulin-like growth factor 1 records.^[8,5]

One naming trap is worth knowing about before searching the literature. A body of work on cognition in older adults, published under the heading growth hormone-releasing hormone, in fact administered tesamorelin and names it only inside the methods. A search on the compound name alone misses those papers, and a reader who finds them can easily take them for studies of the natural hormone.^[28]

Tesamorelin structure and sequence

Read along the chain, the sequence is Tyr-Ala-Asp-Ala-Ile-Phe-Thr-Asn-Ser-Tyr-Arg-Lys-Val-Leu-Gly-Gln-Leu-Ser-Ala-Arg-Lys-Leu-Leu-Gln-Asp-Ile-Met-Ser-Arg-Gln-Gln-Gly-Glu-Ser-Asn-Gln-Glu-Arg-Gly-Ala-Arg-Ala-Arg-Leu, ending in an amide. Every residue is an ordinary L-amino acid; there is no D-residue, no 2-aminoisobutyric acid, no cysteine and therefore no disulfide, no lipid diacid and no polyethylene glycol. In that respect it is a much plainer molecule than the engineered peptides it is often shelved beside. The only non-peptide feature is the (3E)-hex-3-enoyl group on the Tyr1 amine: six carbons, a trans double bond between carbons 3 and 4, joined as an amide.^[2,29,1]

The arithmetic checks that the published figures describe the same object, and here it matters because two authoritative records disagree. Summing the 44 residues as a free acid gives C215H357N71O67S; converting the C-terminus to an amide and acylating the N-terminus with hex-3-enoic acid, less the water lost to the new amide bond, lands on C221H366N72O67S at 5135.9 g/mol average and 5132.7166 Da monoisotopic, which is PubChem's record for CID 16137828 to four decimal places. The FDA registry's own properties read C221H365N71O69S and 5040 Da, both explicitly flagged ESTIMATED, and neither matches the structure that record's modification table describes. A figure copied from that field would be wrong by close to 100 g/mol. A third record disagrees in a way that is easier to miss, because it is a hash rather than a number: the InChIKey published in the encyclopedia infobox for this compound, VQFDKKWXORFBDI-VAVVJCQZSA-N, resolves in PubChem to CID 91886675 at C220H364N72O67S and 5122 g/mol. That is one CH2 short of the molecule described here, which is the difference between a six-carbon and a five-carbon acyl chain, so a reader who searches on that key is looking up a different substance.^[1,2,30]

There is nothing to put on screen, and the reason is worth stating rather than hiding. No structure of this peptide has been deposited, PubChem holds no computed conformer for it, and all four deposited structures of the human receptor carry something else. The closest, PDB 7CZ5, holds the unmodified hormone, and its peptide entity is declared with no non-standard monomers, so neither the acyl group nor the C-terminal amide is in the file. It also covers only 28 of the 44 residues, with the receptor's extracellular domain docked in from a separate crystal structure rather than resolved. A picture of the parent hormone would show a receptor-bound helix, which is evidence about neither the free molecule nor the acylated one.^[6,25,15,1]

Set against the other growth hormone-releasing hormone analogues it is shelved beside, the design choices separate cleanly on three axes: how much of the hormone is kept, what was changed in the sequence, and what the protease-resistance strategy is. Tesamorelin keeps all 44 residues and the natural C-terminal amide, changes no residue at all, and defends the Tyr1 amine with a six-carbon acyl group. Sermorelin keeps the first 29 residues, ends in an argininamide, changes no residue, and carries no protection at the N-terminus, so dipeptidyl peptidase IV cleaves it as it cleaves the hormone. CJC-1295 without DAC keeps the same 29 residues and the argininamide but substitutes four of them, a D-alanine at position 2 that the enzyme cannot accept, glutamine at 8, alanine at 15 and leucine at 27, so it defends the same bond by making the residue itself unreadable rather than by capping the amine. CJC-1295 with DAC adds a thirtieth residue, a lysine whose side chain carries a maleimide that reacts with a free protein thiol, which is a half-life strategy of a different kind again: the peptide ends up attached to a plasma protein. Tesamorelin is the only one of the four that keeps the whole hormone, and the only one whose modification sits on an atom the receptor's deepest pocket also contacts.^[31,1,4,14]

Every residue is L apart from the four glycines, which are achiral, and there are no D-amino acids, no non-proteinogenic residues and no alpha,alpha-dialkyl substitutions anywhere in the chain. The single cysteine-free sequence means there is no disulfide; the peptide is linear and uncyclised, with no glycosylation, no lipid diacid, no polyethylene glycol and no metal coordination. The one sulfur is the thioether of Met27. The only stereochemical feature outside the backbone is the E (trans) configuration of the double bond in the hexenoyl group, which is specified in the name and in the registry fragment and is the reason the older literature calls it trans-3-hexenoyl.^[29,2,3]

What studies on Tesamorelin show

Each card names the experimental system and what was measured. A result in one system is not evidence about another.

Why the modification is on residue 1, and what the receptor structures do and do not settle

The receptor is a class B1 G protein-coupled receptor, 423 residues, an extracellular domain sitting on a seven-helix bundle. The cryo-EM structure of it with the natural hormone and Gs shows the canonical arrangement for the family: the peptide's C-terminal half is held by the extracellular domain while its N-terminal end reaches into the bundle, and a receptor construct lacking that domain nearly abolished cAMP signalling. The output is not single, either: a splice variant differing only at the receptor's own N-terminus couples selectively to beta-arrestins rather than Gs.^{[24,25,32,15]}

Against that picture, the position tesamorelin modifies is a pointed choice. Residue 1 is the deepest residue in the bundle, and the structure assigns it specific contacts: a hydrogen bond from the tyrosine hydroxyl to H210(3.37b), van der Waals contacts to T213(3.40b) and W282(5.36b), and a hydrogen bond from the Tyr1 main-chain NH to R357(7.38b) alongside a bridging water reaching N346(6.57b). It is also the residue whose amine dipeptidyl peptidase IV requires: the enzyme removes Tyr1-Ala2 in one step, at the same rate whether the chain is 44, 29 or 20 residues long, and analogues whose Tyr1 amine is removed or methylated are not cleaved at all. So the hexenoyl group is placed on the one atom that both the protease and the receptor's deepest pocket care about.^[25,4,14,33]

What follows from that is a genuine gap rather than a conclusion. The protease half is reported: the acylated peptide is described as resistant to the enzyme and as degrading more slowly in three species' plasma. The receptor half is not measured anywhere that could be found. There is no published affinity or potency figure for the acylated molecule at this receptor, no structure showing the acyl group in or near the pocket, and no study comparing the two molecules side by side in a binding or cAMP assay. Whether the hexenoyl chain is tolerated in that pocket, displaced out of it, or shed before binding is not established by any source read here. The analytical literature is the one place the intact molecule is routinely handled as itself: four independent methods identify it in urine or plasma by mass, down to the picogram per millilitre range, and one of them notes plainly that this class is characterised by in vivo instability, rapid renal clearance and low urinary concentrations.^{[3,19,20,21,17]}

What is still unknown about Tesamorelin

The receptor-level pharmacology of this specific molecule is missing from the public record. Searches combining the compound and development-code names with receptor, binding, potency and cAMP terms returned 33 records, every one of them clinical, analytical or review material, and the Guide to Pharmacology ligand record that would curate affinity values was refused for want of a registered API key. The five deposited structures of this receptor and its splice variant all carry the natural hormone or a different ligand. So everything structural and quantitative on this page about the binding site is about the parent hormone, with the analogue's single modification sitting on the residue that site grips most tightly.^{[6,15,16,34,32]}

The defining chemical claim rests on one abstract. That the trans-3-hexenoyl group confers resistance to dipeptidyl peptidase IV is stated in the 2007 non-clinical report and, as far as could be established, nowhere else: a PubMed search pairing hexenoyl with growth hormone-releasing factor terms returns exactly that one record. The supporting enzymology is strong but indirect, since it was done on the natural hormone and on analogues modified at Tyr1 in other ways, and the degradation measurements behind the claim used an immunoassay rather than mass spectrometry, so a cleaved fragment retaining the antibody epitope would not have been distinguished from the intact molecule.^[3,4,14]

No in vitro cell study of the molecule was located, which is unusual for a peptide this well characterised clinically. A search restricted to cell, adipocyte, hepatocyte, lipolysis and receptor terms returned fourteen records, all human studies, reviews or analytical methods. So the readings specific to the compound are a liver transcriptome, three plasma proteins, two pharmacokinetic models, one imaging proxy for adipocyte size, and a set of mass-spectrometric identifications. Several of those are not independent of each other: the two liver studies share one small set of participants, the two pharmacokinetic analyses share one phase I population, and the adipose-density reading comes from a responder-restricted pooled post hoc analysis. Stability of the purified peptide outside a biological matrix is unaddressed too: the one stability experiment in this literature, showing rapid degradation above 4 degrees Celsius and below pH 7, was performed on sermorelin and its metabolite and cannot be read across.^{[18,22,23,26,35,36]}

Two last limits. A 12-week randomised placebo-controlled study found no difference between groups in the prespecified insulin response during a glucose tolerance test; it is small and short, so it is weak evidence either way, but it is the only such reading located and is reported rather than omitted. And the corpus is bibliographically scattered: a controlled trial in older adults is indexed and titled under growth hormone-releasing hormone while administering this analogue, so searches on the compound name alone under-recover it. Search the hormone's name, the development code and the compound name together.^[37,28,38]

Key papers on Tesamorelin

1. Structural basis for activation of the growth hormone-releasing hormone receptor.

   Zhou F, Zhang H, Cong Z, Zhao LH, Zhou Q, Mao C, Cheng X, Shen DD, Cai X, Ma C, Wang Y, Dai A, Zhou Y, Sun W, Zhao F, Zhao S, Jiang H, Jiang Y, Yang D, Xu HE, Zhang Y, Wang MW (2020), Nature Communications · Cryo-EM structure with mutagenesis and cAMP assays

   The best picture of how this sequence is held by its receptor, at 2.6 Angstrom with mutagenesis testing the contacts. Open access. It is the natural hormone, not the analogue, which is exactly the point to keep hold of.

2. Dipeptidylpeptidase IV and trypsin-like enzymatic degradation of human growth hormone-releasing hormone in plasma.

   Frohman LA, Downs TR, Heimer EP, Felix AM (1989), The Journal of Clinical Investigation · Plasma enzymology with inhibitors and analogues

   Establishes the cleavage the design exists to prevent: a single dipeptidyl peptidase IV cut at the 2-3 bond, identified with an inhibitor and confirmed as the major circulating species in vivo.

3. Non-clinical pharmacology and safety evaluation of TH9507, a human growth hormone-releasing factor analogue.

   Ferdinandi ES, Brazeau P, High K, Procter B, Fennell S, Dubreuil P (2007), Basic & Clinical Pharmacology & Toxicology · Non-clinical pharmacology and safety evaluation

   THE SINGLE SOURCE for this molecule's defining chemical property, and the only account anywhere of why it carries the group it does. Read it knowing that: a PubMed search pairing hexenoyl with growth hormone-releasing factor terms returns this one record, the degradation measurements behind the claim used an immunoassay rather than mass spectrometry, and no independent replication was located.

4. Kinetics of dipeptidyl peptidase IV proteolysis of growth hormone-releasing factor and analogs.

   Bongers J, Lambros T, Ahmad M, Heimer EP (1992), Biochimica et Biophysica Acta · Enzyme kinetics on a substituted analogue series

   The kinetics behind the chemistry, including the result that modifying the Tyr1 amine stops the enzyme completely while shortening the chain does not change its rate.

5. Advances in the detection of growth hormone releasing hormone synthetic analogs.

   Memdouh S, Gavrilović I, Ng K, Cowan D, Abbate V (2021), Drug Testing and Analysis · In vitro metabolism with LC-MS/MS method development

   Where identity of real material is actually settled: nineteen metabolites synthesised as reference standards for four GHRH analogues, and a candid statement of how little is known about their metabolism.

6. Metabolic effects of a growth hormone-releasing factor in patients with HIV.

   Falutz J, Allas S, Blot K, Potvin D, Kotler D, Somero M, Berger D, Brown S, Richmond G, Fessel J, Turner R, Grinspoon S (2007), The New England Journal of Medicine · Randomised placebo-controlled trial

   The trial that put the molecule in the literature, and the measurement showing it engages the growth hormone axis in humans. Everything later written about it traces back here.

7. Effects of tesamorelin on hepatic transcriptomic signatures in HIV-associated NAFLD.

   Fourman LT, Billingsley JM, Agyapong G, Ho Sui SJ, Feldpausch MN, Purdy J, Zheng I, Pan CS, Corey KE, Torriani M, Kleiner DE, Hadigan CM, Stanley TL, Chung RT, Grinspoon SK (2020), JCI Insight · Hepatic transcriptomics on trial specimens

   The most molecular of the human studies: hepatic gene sets from paired biopsy specimens, which is the closest anything comes to a tissue-level mechanism for this compound.

8. Constitutive signal bias mediated by the human GHRHR splice variant 1.

   Cong Z, Zhou F, Zhang C, Zou X, Zhang H, Wang Y, Zhou Q, Cai X, Liu Q, Li J, Shao L, Mao C, Wang X, Wu J, Xia T, Zhao LH, Jiang H, Zhang Y, Xu HE, Cheng X, Yang D, Wang MW (2021), Proceedings of the National Academy of Sciences of the United States of America · Cryo-EM and signalling study of a receptor splice variant

   Read for the receptor rather than the ligand: it shows that this receptor has a splice variant coupling to beta-arrestins instead of Gs, which is why a single potency figure would not settle what the receptor does.

References

1. 1.PubChem, National Center for Biotechnology Information. Compound Summary CID 16137828, Tesamorelin. PubChem. source · database record
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4. 4.Frohman LA, Downs TR, Heimer EP, Felix AM. (1989). Dipeptidylpeptidase IV and trypsin-like enzymatic degradation of human growth hormone-releasing hormone in plasma. The Journal of Clinical Investigation. 83:1533-1540. doi:10.1172/JCI114049 · abstract only
5. 5.Falutz J, Allas S, Blot K, Potvin D, Kotler D, Somero M, Berger D, Brown S, Richmond G, Fessel J, Turner R, Grinspoon S. (2007). Metabolic effects of a growth hormone-releasing factor in patients with HIV. The New England Journal of Medicine. 357:2359-2370. doi:10.1056/NEJMoa072375 · abstract only
6. 6.Zhou F, Zhang H, Cong Z, Zhao LH, Zhou Q, Mao C, Cheng X, Shen DD, Cai X, Ma C, Wang Y, Dai A, Zhou Y, Sun W, Zhao F, Zhao S, Jiang H, Jiang Y, Yang D, Xu HE, Zhang Y, Wang MW. (2020). Cryo-EM structure of the human growth hormone-releasing hormone receptor-Gs protein complex. RCSB Protein Data Bank, entry 7CZ5. doi:10.2210/pdb7CZ5/pdb · database record
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15. 15.Pike ACW, Quigley A, Barr AJ, Burgess Brown N, Shrestha L, Yang J, Chaikuad A, Vollmar M, Muniz JRC, von Delft F, Edwards A, Arrowsmith CH, Weigelt J, Bountra C, Carpenter EP. Crystal Structure of the Extracellular Domain of Human Growth Hormone Releasing Hormone Receptor. RCSB Protein Data Bank, entry 2XDG. doi:10.2210/pdb2XDG/pdb · database record
16. 16.Wang MW, Hang K, Qiu Y, Chen X, Chen Y, Huang S, Cong Z, Zhou Q. (2026). Cryo-EM structure of the PCO371-bound GHRHR-Gs complex. RCSB Protein Data Bank, entry 24TI. doi:10.2210/pdb24TI/pdb · database record
17. 17.Memdouh S, Gavrilović I, Ng K, Cowan D, Abbate V. (2021). Advances in the detection of growth hormone releasing hormone synthetic analogs. Drug Testing and Analysis. 13:1871-1887. doi:10.1002/dta.3183 · abstract only
18. 18.Coppieters G, Deventer K, Polet M, Van Eenoo P, Judák P. (2022). An antibody-free, ultrafiltration-based assay for the detection of growth hormone-releasing hormones in urine at low pg/mL concentrations using nanoLC-HRMS/MS. Journal of Pharmaceutical and Biomedical Analysis. 214:114726. doi:10.1016/j.jpba.2022.114726 · abstract only
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20. 20.Cristea CD, Radu M, Toboc A, Stan C, David V. (2023). Cationic exchange SPE combined with triple quadrupole UHPLC-MS/MS for detection of GHRHs in urine samples. Analytical Biochemistry. 682:115336. doi:10.1016/j.ab.2023.115336 · abstract only
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22. 22.Fourman LT, Billingsley JM, Agyapong G, Ho Sui SJ, Feldpausch MN, Purdy J, Zheng I, Pan CS, Corey KE, Torriani M, Kleiner DE, Hadigan CM, Stanley TL, Chung RT, Grinspoon SK. (2020). Effects of tesamorelin on hepatic transcriptomic signatures in HIV-associated NAFLD. JCI Insight. 5:e140134. doi:10.1172/jci.insight.140134 · full text read
23. 23.Fourman LT, Stanley TL, Billingsley JM, Sui SJH, Feldpausch MN, Boutin A, Zheng I, McClure CM, Corey KE, Torriani M, Kleiner DE, Hadigan CM, Chung RT, Grinspoon SK. (2021). Delineating tesamorelin response pathways in HIV-associated NAFLD using a targeted proteomic and transcriptomic approach. Scientific Reports. 11:10485. doi:10.1038/s41598-021-89966-y · abstract only
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26. 26.González-Sales M, Barrière O, Tremblay PO, Nekka F, Mamputu JC, Boudreault S, Tanguay M. (2015). Population pharmacokinetic analysis of tesamorelin in HIV-infected patients and healthy subjects. Clinical Pharmacokinetics. 54:285-294. doi:10.1007/s40262-014-0202-x · abstract only
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30. 30.National Center for Biotechnology Information. (2026). PubChem Compound Summary for CID 91886675, C220H364N72O67S, 5122 g/mol: the record the InChIKey published in the encyclopedia infobox for this compound resolves to. Read 3 November 2026. PubChem. source · database record
31. 31.National Center for Biotechnology Information. (2026). PubChem Compound records for the three comparator growth hormone-releasing hormone analogues read for the comparison in this entry: CID 16132413 (sermorelin, C149H246N44O42S, 3357.9), CID 56841945 (CJC-1295 without DAC, C152H252N44O42, 3367.9) and CID 91971820 (CJC-1295 with DAC, C165H269N47O46, 3647.2). Read 3 November 2026. PubChem. source · database record
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34. 34.Cong Z, Zhou F, Zhang C, Zou X, Zhang H, Wang Y, Zhou Q, Cai X, Liu Q, Li J, Shao L, Mao C, Wang X, Wu J, Xia T, Zhao LH, Jiang H, Zhang Y, Xu HE, Cheng X, Yang D, Wang MW. (2021). Cryo-EM structure of the GHRH-bound human GHRHR splice variant 1 complex. RCSB Protein Data Bank, entry 7V9M. doi:10.2210/pdb7V9M/pdb · database record
35. 35.González-Sales M, Barrière O, Tremblay PO, Nekka F, Mamputu JC, Boudreault S, Tanguay M. (2015). Population pharmacokinetic and pharmacodynamic analysis of tesamorelin in HIV-infected patients and healthy subjects. Journal of Pharmacokinetics and Pharmacodynamics. 42:287-299. doi:10.1007/s10928-015-9416-2 · abstract only
36. 36.Lake JE, La K, Erlandson KM, Adrian S, Yenokyan G, Scherzinger A, Dubé MP, Stanley T, Grinspoon S, Falutz J, Mamputu JC, Marsolais C, McComsey GA, Brown TT. (2021). Tesamorelin improves fat quality independent of changes in fat quantity. AIDS. 35:1395-1402. doi:10.1097/QAD.0000000000002897 · abstract only
37. 37.Clemmons DR, Miller S, Mamputu JC. (2017). Safety and metabolic effects of tesamorelin, a growth hormone-releasing factor analogue, in patients with type 2 diabetes: A randomized, placebo-controlled trial. PLoS One. 12:e0179538. doi:10.1371/journal.pone.0179538 · abstract only
38. 38.Makimura H, Murphy CA, Feldpausch MN, Grinspoon SK. (2014). The effects of tesamorelin on phosphocreatine recovery in obese subjects with reduced GH. The Journal of Clinical Endocrinology and Metabolism. 99:338-343. doi:10.1210/jc.2013-3436 · abstract only
39. 39.Jansen M, Darby I, Abribat T, Dubreuil P, Ferdinandi ES, Hardy JG. (2004). Pulmonary delivery of TH9507, a growth hormone releasing factor analogue, in the dog. International Journal of Pharmaceutics. 276:75-81. doi:10.1016/j.ijpharm.2004.02.012 · abstract only
40. 40.US Food and Drug Administration, Global Substance Registration System. TESAMORELIN ACETATE, substance record (UNII LGW5H38VE3). FDA Global Substance Registration System. source · database record
41. 41.Kanehisa Laboratories. (2026). KEGG DRUG entries D06655 (Tesamorelin, USAN) and D09015 (Tesamorelin acetate, USAN). Read 3 November 2026. KEGG DRUG. source · database record
42. 42.Wang MW, Hang K, Qiu Y, Chen X, Chen Y, Huang S, Cong Z, Zhou Q. (2026). Cryo-EM structure of the ligand-free (Apo) GHRHR-Gs complex. RCSB Protein Data Bank, entry 24TB. doi:10.2210/pdb24TB/pdb · database record