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Tesamorelin / Studies
Modified form · 44 amino acids · 5,135.9 Da

Tesamorelin studies and research data

PepBank has 50 tesamorelin studies with results. 42 of them gave tesamorelin, with 288 results, grouped by what the studies measured. In each group, results from studies in people come first. Data as of 2026-10-30.

Searches 288 results and 109 papers. Newer studies from Europe PMC

Results in people
256
89% of 288 results
Results in animals
30
10% of 288 results
Results in lab cells
2
under 1% of 288 results
From computer models
0
0% of 288 results
The molecule

Tesamorelin identity

Identifiers, parent molecule, targets and development stage, from curated data.

Tesamorelin is human growth hormone-releasing factor 1-44 amide with a (3E)-hex-3-enoyl group on the N-terminal tyrosine. In laboratory studies the acyl cap made the peptide resistant to dipeptidyl peptidase-IV (PMID 17214611). The FDA label states that tesamorelin binds and stimulates human GRF receptors with similar potency to the endogenous GRF; it stimulates growth hormone secretion and so raises IGF-1. FDA approved it in 2010 (BLA 022505, Theratechnologies) for reduction of excess abdominal fat in HIV-infected adults with lipodystrophy; the current products are EGRIFTA SV and EGRIFTA WR (WR approved by supplement in March 2025). The EU application was withdrawn in 2012 before authorisation.

Kind
Modified form · 44 residues
Identifiers
ChEMBLCHEMBL1237026 (opens in a new tab)CHEMBL2111290 (opens in a new tab)PubChem CID16137828 (opens in a new tab)UNIIMQG94M5EEO (opens in a new tab)LGW5H38VE3 (opens in a new tab)DrugBankDB08869 (opens in a new tab)CAS218949-48-5901758-09-6KEGGD06655 (opens in a new tab)D09015 (opens in a new tab)IUPHAR6959 (opens in a new tab)
Parent
Modified form of Somatorelin, human GHRH(1-44) · residues 32-75The peptide chain is identical to mature human somatoliberin 1-44 with the C-terminal leucinamide; the only change is the added (3E)-hex-3-enoyl group on Tyr1. GSRS reports an exact duplicate sequence between the tesamorelin and somatorelin subunits, and the FDA label calls tesamorelin 'a human growth hormone-releasing factor (GRF) analog ... comprised of the 44 amino acid sequence of human GRF and a hexenoyl moiety'.
Development
Approved in the US (Egrifta, 2010)Theratechnologies Inc. (Montreal). Secondary reports say CB Biotechnology, an affiliate of Future Pak, completed its acquisition of Theratechnologies on 2025-09-25; the FDA label of 2026-07-29 still names Theratechnologies Inc. as the manufacturer.ChEMBL records max_phase 4 and first approval 2010. Later work is mostly investigator-led: open phase 2 studies include NCT06554717 (physical function in HIV, Massachusetts General Hospital, recruiting, start 2025-07-10) and NCT03150511 (peripheral nerve injury, Johns Hopkins, recruiting). Two of the 24 ClinicalTrials.gov records need care. NCT07481734 is titled '(Mock Study)' and should not be read as a real trial. NCT00257712 (University of Washington, phase 2, completed) names the drug only by its code name TH9507, so the count needs the code name. Source (opens in a new tab)

Targets

Molecular targets with action and evidence source
TargetActionEvidence
Growth hormone-releasing hormone receptorGHRHRQ02643 (opens in a new tab)Agonistapproved-drug labelSource (opens in a new tab)

Sequence and structure

Residues, differences from the parent, calculated properties and 3D structure. Source values and calculated values are shown separately.

Sequence

44 amino acids · 2 modifications

Residues 1 to 10:
ADAIFTNSY
Residues 11 to 20:
RKVLGQLSAR
Residues 21 to 30:
KLLQDIMSRQ
Residues 31 to 40:
QGESNQERGA
Residues 41 to 44:
RARL
  • HydrophobicA V I L M
  • AromaticF W Y
  • PositiveK R H
  • NegativeD E
  • PolarS T N Q
  • SpecialC G P
  • Modified residue

Modifications

Tyr1 N-terminus
Other modification
(3E)-hex-3-enoyl group, a C6 acyl chain with a double bond at position 3, on the N-terminal tyrosine. The FDA label states 'a hexenoyl moiety, a C6 chain with a double bond at position 3, attached to the tyrosine residue at the N-terminal part of the molecule'. GSRS records it as the fragment '3-HEXENOYL TYROSINE, (3E)-' (UNII 09PC85U6VI) at residue 1. Not an acetyl cap, so n_terminal_acetylation does not apply.
Leu44-NH2
C-terminal amide
C-terminal leucinamide, as in native somatoliberin (UniProt P01286 modified residue 75, 'Leucine amide').

Alignment to Somatorelin, human GHRH(1-44)

Calculated from the two sequences. Curated notes are shown as given.

44 of 44 aligned residues identical (100%) · 2 modified residues · Somatorelin, human GHRH(1-44) 1–44

  • Top row: Somatorelin, human GHRH(1-44) (parent)
  • Bottom row: Tesamorelin
ADAIFTNSY
RKVLGQLSAR
KLLQDIMSRQ
QGESNQERGA
RAR
  • Same as parent
  • Substituted
  • Non-canonical or D-form
  • Added
  • Gap
  • Modified side chain or end

Differences from the parent

  1. 1Parent 1 · analog 1Tyr, modified · Other modification(3E)-hex-3-enoyl group, a C6 acyl chain with a double bond at position 3, on the N-terminal tyrosine. The FDA label states 'a hexenoyl moiety, a C6 chain with a double bond at position 3, attached to the tyrosine residue at the N-terminal part of the molecule'. GSRS records it as the fragment '3-HEXENOYL TYROSINE, (3E)-' (UNII 09PC85U6VI) at residue 1. Not an acetyl cap, so n_terminal_acetylation does not apply.
  2. 2Parent 44 · analog 44Leu, modified · C-terminal amideC-terminal leucinamide, as in native somatoliberin (UniProt P01286 modified residue 75, 'Leucine amide').

Basis: The peptide chain is identical to mature human somatoliberin 1-44 with the C-terminal leucinamide; the only change is the added (3E)-hex-3-enoyl group on Tyr1. GSRS reports an exact duplicate sequence between the tesamorelin and somatorelin subunits, and the FDA label calls tesamorelin 'a human growth hormone-releasing factor (GRF) analog ... comprised of the 44 amino acid sequence of human GRF and a hexenoyl moiety'.

Calculated from the two sequences with @pepdb/chem alignToParent (ungapped unless a gap scores higher). The record’s curated notes are shown as given.

Properties

From identity sources

Formula
C221H366N72O67S
Molecular weight
5,135.9 g/mol
Monoisotopic mass
5,132.7166 Da

Calculated from the sequence

Some values cannot be calculated. A modification changes this value and is not modeled here (for example a lipid, metal or linker).

Average mass
Not calculated
Monoisotopic mass
Not calculated
Isoelectric point (pI)
Not calculated
Net charge at pH 7.4
Not calculated
GRAVY (hydropathy)
−0.798
Mean Kyte-Doolittle hydropathy · Kyte and Doolittle 1982
Negative: hydrophilic on average.
Extinction coefficient, 280 nm (Cys reduced)
2,980 M⁻¹ cm⁻¹
5500 x Trp + 1490 x Tyr · Pace et al. 1995 (ExPASy ProtParam)
No Trp: ExPASy reports more than 10 % error without Trp.
Instability index
38.48
Dipeptide instability weights (DIWV) · Guruprasad et al. 1990
40 or below: classed as stable (ExPASy).
Aliphatic index
80.0
Mole % A + 2.9 V + 3.9 (I + L) · Ikai 1980
Boman index
3.03 kcal/mol
Mean solubility value (negated) · Boman 2003
Above 2.48: high protein-binding potential (Boman).
Hydrophobic moment (μH)
0.612
Eisenberg scale, 100° per residue, best 11-residue window · Eisenberg et al. 1982, 1984
  • Not included: other modification. Mass, charge and pI are not calculated; use the identity-source values.
  • The N-terminal group is not modeled.
  • Defined and validated for proteins; use with care for short peptides.
  • Assumes an ideal alpha helix. Many short peptides are not helical.

@pepdb/chem 0.2.0 · EMBOSS pKa set · ExPASy residue masses

Net charge by pH

No charge curve

A modification changes this value and is not modeled here (for example a lipid, metal or linker).

Composition

  • Hydrophobic32% (14)
  • Aromatic7% (3)
  • Positive18% (8)
  • Negative9% (4)
  • Polar27% (12)
  • Special7% (3)

44 residues. Each residue counts in one class; F and W count as aromatic.

A Ala5 · 11%
I Ile2 · 5%
L Leu5 · 11%
M Met1 · 2%
V Val1 · 2%
F Phe1 · 2%
W Trp0 · 0%
Y Tyr2 · 5%
H His0 · 0%
K Lys2 · 5%
R Arg6 · 14%
D Asp2 · 5%
E Glu2 · 5%
N Asn2 · 5%
Q Gln5 · 11%
S Ser4 · 9%
T Thr1 · 2%
C Cys0 · 0%
G Gly3 · 7%
P Pro0 · 0%

3D structure

PredictedAlphaFold DB · P01286

Loads the 3D viewer (3Dmol.js, about 150 KB) and the model file from AlphaFold DB (EMBL-EBI).

  • Very high (pLDDT > 90)
  • Confident (90 > pLDDT > 70)
  • Low (70 > pLDDT > 50)
  • Very low (pLDDT < 50)

Predicted model of the whole UniProt entry P01286, not an experimental structure of Tesamorelin. Tesamorelin = residues 32–75.

AlphaFold DB, EMBL-EBI and Google DeepMind · CC BY 4.0

2D structure

Tesamorelin has 44 residues. A full-atom drawing is hard to read at this size; the sequence view is the reference.

SMILES fromPubChem CID 16137828(opens in a new tab)

CC/C=C/CC(=O)N[C@@H](CC1=CC=C(C=C1)O)C(=O)N[C@@H](C)C(=O)N[C@@H](CC(=O)O)C(=O)N[C@@H](C)C(=O)N[C@@H]([C@@H](C)CC)C(=O)N[C@@H](CC2=CC=CC=C2)C(=O)N[C@@H]([C@@H](C)O)C(=O)N[C@@H](CC(=O)N)C(=O)N[C@@H](CO)C(=O)N[C@@H](CC3=CC=C(C=C3)O)C(=O)N[C@@H](CCCNC(=N)N)C(=O)N[C@@H](CCCCN)C(=O)N[C@@H](C(C)C)C(=O)N[C@@H](CC(C)C)C(=O)NCC(=O)N[C@@H](CCC(=O)N)C(=O)N[C@@H](CC(C)C)C(=O)N[C@@H](CO)C(=O)N[C@@H](C)C(=O)N[C@@H](CCCNC(=N)N)C(=O)N[C@@H](CCCCN)C(=O)N[C@@H](CC(C)C)C(=O)N[C@@H](CC(C)C)C(=O)N[C@@H](CCC(=O)N)C(=O)N[C@@H](CC(=O)O)C(=O)N[C@@H]([C@@H](C)CC)C(=O)N[C@@H](CCSC)C(=O)N[C@@H](CO)C(=O)N[C@@H](CCCNC(=N)N)C(=O)N[C@@H](CCC(=O)N)C(=O)N[C@@H](CCC(=O)N)C(=O)NCC(=O)N[C@@H](CCC(=O)O)C(=O)N[C@@H](CO)C(=O)N[C@@H](CC(=O)N)C(=O)N[C@@H](CCC(=O)N)C(=O)N[C@@H](CCC(=O)O)C(=O)N[C@@H](CCCNC(=N)N)C(=O)NCC(=O)N[C@@H](C)C(=O)N[C@@H](CCCNC(=N)N)C(=O)N[C@@H](C)C(=O)N[C@@H](CCCNC(=N)N)C(=O)N[C@@H](CC(C)C)C(=O)N

Helical wheel

An ideal alpha-helix projection. It shows where the hydrophobic residues fall if the peptide folds as a helix. It does not show that it does.

Helical wheel of Tesamorelin, 44 residues at 100 degrees per residue. Hydrophobic moment 0.04 pointing at 52 degrees.Tyr 1, Eisenberg consensus (normalized) 0.26Y1Ala 2, Eisenberg consensus (normalized) 0.62A2Asp 3, Eisenberg consensus (normalized) -0.90D−3Ala 4, Eisenberg consensus (normalized) 0.62A4Ile 5, Eisenberg consensus (normalized) 1.38I5Phe 6, Eisenberg consensus (normalized) 1.19F6Thr 7, Eisenberg consensus (normalized) -0.05T7Asn 8, Eisenberg consensus (normalized) -0.78N8Ser 9, Eisenberg consensus (normalized) -0.18S9Tyr 10, Eisenberg consensus (normalized) 0.26Y10Arg 11, Eisenberg consensus (normalized) -2.53R+11Lys 12, Eisenberg consensus (normalized) -1.50K+12Val 13, Eisenberg consensus (normalized) 1.08V13Leu 14, Eisenberg consensus (normalized) 1.06L14Gly 15, Eisenberg consensus (normalized) 0.48G15Gln 16, Eisenberg consensus (normalized) -0.85Q16Leu 17, Eisenberg consensus (normalized) 1.06L17Ser 18, Eisenberg consensus (normalized) -0.18S18Ala 19, Eisenberg consensus (normalized) 0.62A19Arg 20, Eisenberg consensus (normalized) -2.53R+20Lys 21, Eisenberg consensus (normalized) -1.50K+21Leu 22, Eisenberg consensus (normalized) 1.06L22Leu 23, Eisenberg consensus (normalized) 1.06L23Gln 24, Eisenberg consensus (normalized) -0.85Q24Asp 25, Eisenberg consensus (normalized) -0.90D−25Ile 26, Eisenberg consensus (normalized) 1.38I26Met 27, Eisenberg consensus (normalized) 0.64M27Ser 28, Eisenberg consensus (normalized) -0.18S28Arg 29, Eisenberg consensus (normalized) -2.53R+29Gln 30, Eisenberg consensus (normalized) -0.85Q30Gln 31, Eisenberg consensus (normalized) -0.85Q31Gly 32, Eisenberg consensus (normalized) 0.48G32Glu 33, Eisenberg consensus (normalized) -0.74E−33Ser 34, Eisenberg consensus (normalized) -0.18S34Asn 35, Eisenberg consensus (normalized) -0.78N35Gln 36, Eisenberg consensus (normalized) -0.85Q36Glu 37, Eisenberg consensus (normalized) -0.74E−37Arg 38, Eisenberg consensus (normalized) -2.53R+38Gly 39, Eisenberg consensus (normalized) 0.48G39Ala 40, Eisenberg consensus (normalized) 0.62A40Arg 41, Eisenberg consensus (normalized) -2.53R+41Ala 42, Eisenberg consensus (normalized) 0.62A42Arg 43, Eisenberg consensus (normalized) -2.53R+43Leu 44, Eisenberg consensus (normalized) 1.06L44
μH, residues shown
0.044
μH, best 11-residue window
0.612
Arrow direction
52°
Residues
44 · 3 rings of 18
HydrophilicHydrophobic

Eisenberg consensus (normalized) scale · + K, R · − D, E

Assumes an ideal α-helix: 100° per residue, 3.6 residues per turn. The arrow is the mean hydrophobic moment (Eisenberg et al. 1984) and points at the hydrophobic face.

Show as table
PositionResidueAngleEisenberg consensus (normalized)
1Y0°0.26
2A100°0.62
3D200°-0.90
4A300°0.62
5I40°1.38
6F140°1.19
7T240°-0.05
8N340°-0.78
9S80°-0.18
10Y180°0.26
11R280°-2.53
12K20°-1.50
13V120°1.08
14L220°1.06
15G320°0.48
16Q60°-0.85
17L160°1.06
18S260°-0.18
19A0°0.62
20R100°-2.53
21K200°-1.50
22L300°1.06
23L40°1.06
24Q140°-0.85
25D240°-0.90
26I340°1.38
27M80°0.64
28S180°-0.18
29R280°-2.53
30Q20°-0.85
31Q120°-0.85
32G220°0.48
33E320°-0.74
34S60°-0.18
35N160°-0.78
36Q260°-0.85
37E0°-0.74
38R100°-2.53
39G200°0.48
40A300°0.62
41R40°-2.53
42A140°0.62
43R240°-2.53
44L340°1.06
Results by area

What the studies measured

People first in each area, then animals, then lab cells. Counts are exact and come from studies that gave the peptide.

Trials and papers
Status and safety
Data

Compare