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Tirzepatide / Studies
Synthetic analog · 39 amino acids · 4,813.5 Da

Tirzepatide studies and research data

PepBank has 457 tirzepatide studies with results. 378 of them gave tirzepatide, with 2,165 results, grouped by what the studies measured. In each group, results from studies in people come first. Data as of 2026-10-30.

Searches 2,165 results and 2,842 papers. Newer studies from Europe PMC

Results in people
2,050
95% of 2,165 results
Results in animals
68
3% of 2,165 results
Results in lab cells
12
under 1% of 2,165 results
From computer models
35
2% of 2,165 results
The molecule

Tirzepatide identity

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

Tirzepatide is a 39-residue synthetic peptide based on the GIP sequence. It has Aib at positions 2 and 13, a C-terminal amide, and Lys20 linked to a C20 fatty diacid (1,20-eicosanedioic acid) through two AEEA units and L-gamma-Glu; the label states that the diacid enables albumin binding. It activates the GIP and GLP-1 receptors. Eli Lilly developed it; it is approved in the US (Mounjaro, Zepbound) and the EU (Mounjaro) for type 2 diabetes and weight management, and in the US also for obstructive sleep apnea in adults with obesity.

Kind
Synthetic analog · 39 residues
Identifiers
ChEMBLCHEMBL4297839 (opens in a new tab)PubChem CID166567236 (opens in a new tab)UNIIOYN3CCI6QE (opens in a new tab)DrugBankDB15171 (opens in a new tab)CAS2023788-19-2PDB7FIM (opens in a new tab)7FIY (opens in a new tab)7RBT (opens in a new tab)7RGP (opens in a new tab)KEGGD11360 (opens in a new tab)IUPHAR11429 (opens in a new tab)
Parent
Analog of Gastric inhibitory polypeptide (GIP), humanFDA label: 'Tirzepatide is based on the GIP sequence'. Substitutions are a direct alignment of residues 1-30 with human GIP(1-42) from UniProt P09681.
Development
Approved in the US and EU (Mounjaro, 2022)Eli Lilly and CompanyFirst FDA approval 2022-05-13 (Mounjaro, NDA215866, Type 1 new molecular entity). ChEMBL max_phase 4. ClinicalTrials.gov lists 297 studies for query.intr=tirzepatide OR LY3298176. Source (opens in a new tab)The note counts 297 studies from a registry search made when the note was written, with its own search terms. PepBank links 254 registered trials to Tirzepatide today, so the two numbers differ.

Targets

Molecular targets with action and evidence source
TargetActionEvidence
Gastric inhibitory polypeptide receptorGIPRP48546 (opens in a new tab)Agonistapproved-drug labelSource (opens in a new tab)
Glucagon-like peptide 1 receptorGLP1RP43220 (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

39 amino acids · 4 modifications

H-
Residues 1 to 10:
YEGTFTSDY
Residues 11 to 20:
SILDKIAQ
Residues 21 to 30:
AFVQWLIAGG
Residues 31 to 39:
PSSGAPPPS
  • HydrophobicA V I L M
  • AromaticF W Y
  • PositiveK R H
  • NegativeD E
  • PolarS T N Q
  • SpecialC G P
  • Non-canonicalX
  • Modified residue

Modifications

Aib2
Non-canonical residue
2-aminoisobutyric acid (GSRS fragment UNII 1E7ZW41IQU; FDA label).
Aib13
Non-canonical residue
2-aminoisobutyric acid (GSRS; FDA label).
Lys20
Lipidation
N6 carries, from Lys outward: two AEEA units ([2-(2-aminoethoxy)ethoxy]acetyl), L-gamma-Glu, then 19-carboxynonadecanoyl (C20 fatty diacid). GSRS fragment UNII NVV1P9GCY2. FDA label: the C20 diacid enables albumin binding.
Ser39-NH2
C-terminal amide
C-terminal serinamide (GSRS fragment UNII CIJ0MD19SE; FDA label).

Alignment to Gastric inhibitory polypeptide (GIP)

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

19 of 30 aligned residues identical (63%) · 9 substitutions · 2 non-canonical residues · 1 replaced segment · Gastric inhibitory polypeptide (GIP) 1–39

  • Top row: Gastric inhibitory polypeptide (GIP) (parent)
  • Bottom row: Tirzepatide
YEGTFSDY
SIDKIQ
FVWLA
PSSGAPPPS
  • Same as parent
  • Substituted
  • Non-canonical or D-form
  • Added
  • Gap
  • Modified side chain or end
  • Replaced segment
  • Parent context

Differences from the parent

  1. 1Parent 2 · analog 2Ala → Aib · Non-canonical residue2-aminoisobutyric acid (GSRS fragment UNII 1E7ZW41IQU; FDA label).
  2. 2Parent 7 · analog 7Ile → Thr · Substitution
  3. 3Parent 13 · analog 13Ala → Aib · Non-canonical residue2-aminoisobutyric acid (GSRS; FDA label).
  4. 4Parent 14 · analog 14Met → Leu · Substitution
  5. 5Parent 18 · analog 18His → Ala · Substitution
  6. 6Parent 20 · analog 20Gln → Lys · SubstitutionLys20 carries the C20 diacid side chain. N6 carries, from Lys outward: two AEEA units ([2-(2-aminoethoxy)ethoxy]acetyl), L-gamma-Glu, then 19-carboxynonadecanoyl (C20 fatty diacid). GSRS fragment UNII NVV1P9GCY2. FDA label: the C20 diacid enables albumin binding.
  7. 7Parent 21 · analog 21Asp → Ala · Substitution
  8. 8Parent 24 · analog 24Asn → Gln · Substitution
  9. 9Parent 27 · analog 27Leu → Ile · Substitution
  10. 10Parent 29 · analog 29Gln → Gly · Substitution
  11. 11Parent 30 · analog 30Lys → Gly · Substitution
  12. 12Parent 31–42 · analog 31–39GKKNDWKHNITQ → PSSGAPPPS · Segment replacedC-terminal segment differs; tirzepatide has 39 residues and a C-terminal amide.

Basis: FDA label: 'Tirzepatide is based on the GIP sequence'. Substitutions are a direct alignment of residues 1-30 with human GIP(1-42) from UniProt P09681.

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
C225H348N48O68
Molecular weight
4,813.53 g/mol
Monoisotopic mass
4,810.5249 Da

Calculated from the sequence

Some values cannot be calculated. The sequence has a non-canonical residue (X). Residue tables cover only the 20 standard amino acids.

Average mass
Not calculated
Monoisotopic mass
Not calculated
Isoelectric point (pI)
Not calculated
Net charge at pH 7.4
Not calculated
GRAVY (hydropathy)
Not calculated
Extinction coefficient, 280 nm (Cys reduced)
8,480 M⁻¹ cm⁻¹
5500 x Trp + 1490 x Tyr · Pace et al. 1995 (ExPASy ProtParam)
Instability index
Not calculated
Aliphatic index
Not calculated
Boman index
Not calculated
Hydrophobic moment (μH)
Not calculated
  • 2 non-canonical residues (X) are not included in calculated values.
  • Not included: lipid chain. Mass, charge and pI are not calculated; use the identity-source values.
  • 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

The sequence has a non-canonical residue (X). Residue tables cover only the 20 standard amino acids.

Composition

  • Hydrophobic26% (10)
  • Aromatic13% (5)
  • Positive5% (2)
  • Negative8% (3)
  • Polar23% (9)
  • Special21% (8)
  • Non-canonical5% (2)

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

A Ala4 · 10%
I Ile3 · 8%
L Leu2 · 5%
M Met0 · 0%
V Val1 · 3%
F Phe2 · 5%
W Trp1 · 3%
Y Tyr2 · 5%
H His0 · 0%
K Lys2 · 5%
R Arg0 · 0%
D Asp2 · 5%
E Glu1 · 3%
N Asn0 · 0%
Q Gln2 · 5%
S Ser5 · 13%
T Thr2 · 5%
C Cys0 · 0%
G Gly4 · 10%
P Pro4 · 10%
X Xaa2 · 5%

3D structure

ExperimentalPDB 7FIM

Loads the 3D viewer (3Dmol.js, about 150 KB) and the model file from RCSB PDB.

RCSB Protein Data Bank · CC0 1.0

2D structure

Tirzepatide has 39 residues. A full-atom drawing is hard to read at this size; the sequence view is the reference.

SMILES fromPubChem CID 166567236(opens in a new tab)

CC[C@H](C)[C@@H](C(=O)N[C@@H](C)C(=O)N[C@@H](CCC(=O)N)C(=O)N[C@@H](CCCCNC(=O)COCCOCCNC(=O)COCCOCCNC(=O)CC[C@@H](C(=O)O)NC(=O)CCCCCCCCCCCCCCCCCCC(=O)O)C(=O)N[C@@H](C)C(=O)N[C@@H](CC1=CC=CC=C1)C(=O)N[C@@H](C(C)C)C(=O)N[C@@H](CCC(=O)N)C(=O)N[C@@H](CC2=CNC3=CC=CC=C32)C(=O)N[C@@H](CC(C)C)C(=O)N[C@@H]([C@@H](C)CC)C(=O)N[C@@H](C)C(=O)NCC(=O)NCC(=O)N4CCC[C@H]4C(=O)N[C@@H](CO)C(=O)N[C@@H](CO)C(=O)NCC(=O)N[C@@H](C)C(=O)N5CCC[C@H]5C(=O)N6CCC[C@H]6C(=O)N7CCC[C@H]7C(=O)N[C@@H](CO)C(=O)N)NC(=O)[C@H](CCCCN)NC(=O)[C@H](CC(=O)O)NC(=O)[C@H](CC(C)C)NC(=O)C(C)(C)NC(=O)[C@H]([C@@H](C)CC)NC(=O)[C@H](CO)NC(=O)[C@H](CC8=CC=C(C=C8)O)NC(=O)[C@H](CC(=O)O)NC(=O)[C@H](CO)NC(=O)[C@H]([C@@H](C)O)NC(=O)[C@H](CC9=CC=CC=C9)NC(=O)[C@H]([C@@H](C)O)NC(=O)CNC(=O)[C@H](CCC(=O)O)NC(=O)C(C)(C)NC(=O)[C@H](CC1=CC=C(C=C1)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 Tirzepatide, 39 residues at 100 degrees per residue. Hydrophobic moment 0.08 pointing at 245 degrees.Tyr 1, Eisenberg consensus (normalized) 0.26Y1Non-canonical 2X2Glu 3, Eisenberg consensus (normalized) -0.74E−3Gly 4, Eisenberg consensus (normalized) 0.48G4Thr 5, Eisenberg consensus (normalized) -0.05T5Phe 6, Eisenberg consensus (normalized) 1.19F6Thr 7, Eisenberg consensus (normalized) -0.05T7Ser 8, Eisenberg consensus (normalized) -0.18S8Asp 9, Eisenberg consensus (normalized) -0.90D−9Tyr 10, Eisenberg consensus (normalized) 0.26Y10Ser 11, Eisenberg consensus (normalized) -0.18S11Ile 12, Eisenberg consensus (normalized) 1.38I12Non-canonical 13X13Leu 14, Eisenberg consensus (normalized) 1.06L14Asp 15, Eisenberg consensus (normalized) -0.90D−15Lys 16, Eisenberg consensus (normalized) -1.50K+16Ile 17, Eisenberg consensus (normalized) 1.38I17Ala 18, Eisenberg consensus (normalized) 0.62A18Gln 19, Eisenberg consensus (normalized) -0.85Q19Lys 20, Eisenberg consensus (normalized) -1.50K+20Ala 21, Eisenberg consensus (normalized) 0.62A21Phe 22, Eisenberg consensus (normalized) 1.19F22Val 23, Eisenberg consensus (normalized) 1.08V23Gln 24, Eisenberg consensus (normalized) -0.85Q24Trp 25, Eisenberg consensus (normalized) 0.81W25Leu 26, Eisenberg consensus (normalized) 1.06L26Ile 27, Eisenberg consensus (normalized) 1.38I27Ala 28, Eisenberg consensus (normalized) 0.62A28Gly 29, Eisenberg consensus (normalized) 0.48G29Gly 30, Eisenberg consensus (normalized) 0.48G30Pro 31, Eisenberg consensus (normalized) 0.12P31Ser 32, Eisenberg consensus (normalized) -0.18S32Ser 33, Eisenberg consensus (normalized) -0.18S33Gly 34, Eisenberg consensus (normalized) 0.48G34Ala 35, Eisenberg consensus (normalized) 0.62A35Pro 36, Eisenberg consensus (normalized) 0.12P36Pro 37, Eisenberg consensus (normalized) 0.12P37Pro 38, Eisenberg consensus (normalized) 0.12P38Ser 39, Eisenberg consensus (normalized) -0.18S39
μH, residues shown
0.079
μH, best 11-residue window
—
Arrow direction
245°
Residues
39 · 3 rings of 18 · 2 X not scored
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
2X100°not scored
3E200°-0.74
4G300°0.48
5T40°-0.05
6F140°1.19
7T240°-0.05
8S340°-0.18
9D80°-0.90
10Y180°0.26
11S280°-0.18
12I20°1.38
13X120°not scored
14L220°1.06
15D320°-0.90
16K60°-1.50
17I160°1.38
18A260°0.62
19Q0°-0.85
20K100°-1.50
21A200°0.62
22F300°1.19
23V40°1.08
24Q140°-0.85
25W240°0.81
26L340°1.06
27I80°1.38
28A180°0.62
29G280°0.48
30G20°0.48
31P120°0.12
32S220°-0.18
33S320°-0.18
34G60°0.48
35A160°0.62
36P260°0.12
37P0°0.12
38P100°0.12
39S200°-0.18
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