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Exenatide (exendin-4) / Studies
Natural peptide · 39 amino acids · 4,187 Da

Exenatide (exendin-4) studies and research data

PepBank has 530 exenatide studies with results. 473 of them gave exenatide, with 3,292 results, grouped by what the studies measured. In each group, results from studies in people come first. Data as of 2026-10-30.

Searches 3,292 results and 1,431 papers. Newer studies from Europe PMC

Results in people
2,193
67% of 3,292 results
Results in animals
955
29% of 3,292 results
Results in lab cells
144
4% of 3,292 results
From computer models
0
0% of 3,292 results
The molecule

Exenatide identity

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

Exenatide is a 39-residue peptide with the sequence of exendin-4 from Gila monster venom. Commercial manufacture uses peptide synthesis. This natural_peptide classification describes sequence origin. Byetta is immediate release. Bydureon uses extended release. Labeled exendin imaging probes are different chemical products.

Kind
Natural peptide · 39 residues
Identifiers
PubChem CID45588096 (opens in a new tab)UNII9P1872D4OL (opens in a new tab)CAS141758-74-9
Development
Approved in the US (Byetta)Amylin Pharmaceuticals and partnersAn approved medicinal product exists. Investigational indications and formulations have separate development status. Source (opens in a new tab)

Targets

Molecular targets with action and evidence source
TargetActionEvidence
Glucagon-like peptide-1 receptorGLP1RP43220 (opens in a new tab)Agonistofficial prescribing informationSource (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 · 1 modification

H-
Residues 1 to 10:
HGEGTFTSDL
Residues 11 to 20:
SKQMEEEAVR
Residues 21 to 30:
LFIEWLKNGG
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
  • Modified residue

Modifications

39
C-terminal amide
C-terminal carboxamide.

Properties

From identity sources

Formula
C184H282N50O60S
Molecular weight
4,187 g/mol
Monoisotopic mass
4,184.0273 Da

Calculated from the sequence

Average mass
4,186.62 Da
Sum of ExPASy residue masses + water + C-amide · ExPASy Compute pI/Mw; FindMod
Monoisotopic mass
4,184.0272 Da
Sum of ExPASy residue masses + water + C-amide · ExPASy FindMod
Isoelectric point (pI)
4.76
pH of zero net charge, EMBOSS pKa set · EMBOSS iep, Epk.dat
Net charge at pH 7.4
−1.95
Henderson-Hasselbalch, EMBOSS pKa set · EMBOSS iep, Epk.dat
GRAVY (hydropathy)
−0.692
Mean Kyte-Doolittle hydropathy · Kyte and Doolittle 1982
Negative: hydrophilic on average.
Extinction coefficient, 280 nm (Cys reduced)
5,500 M⁻¹ cm⁻¹
5500 x Trp + 1490 x Tyr · Pace et al. 1995 (ExPASy ProtParam)
Instability index
64.08
Dipeptide instability weights (DIWV) · Guruprasad et al. 1990
Above 40: classed as possibly unstable (ExPASy).
Aliphatic index
52.6
Mole % A + 2.9 V + 3.9 (I + L) · Ikai 1980
Boman index
1.67 kcal/mol
Mean solubility value (negated) · Boman 2003
2.48 or below: lower protein-binding potential (Boman).
Hydrophobic moment (μH)
0.708
Eisenberg scale, 100° per residue, best 11-residue window · Eisenberg et al. 1982, 1984
pI with each pKa set
EMBOSS 4.76Bjellqvist (ExPASy) 5.04IPC peptide 4.92IPC protein 4.96
  • 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

pI 4.76 · Net charge at pH 7.4: −1.95

Point or use arrow keys

Net charge of Exenatide (exendin-4) from pH 0 to 14 (EMBOSS pKa set). Isoelectric point 4.76. Net charge at pH 7.4: -1.95.−10−50+502468101214pHNet chargepH 7.4pI 4.76

Henderson-Hasselbalch, EMBOSS pKa set, C-amide. Calculated, not measured.

Show as table
pHNet charge
05.00
14.99
24.95
34.52
42.23
5−0.40
6−1.17
7−1.78
8−2.17
9−2.74
10−3.24
11−4.25
12−5.12
13−5.75
14−5.97

Composition

  • Hydrophobic21% (8)
  • Aromatic8% (3)
  • Positive10% (4)
  • Negative15% (6)
  • Polar23% (9)
  • Special23% (9)

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

A Ala2 · 5%
I Ile1 · 3%
L Leu3 · 8%
M Met1 · 3%
V Val1 · 3%
F Phe2 · 5%
W Trp1 · 3%
Y Tyr0 · 0%
H His1 · 3%
K Lys2 · 5%
R Arg1 · 3%
D Asp1 · 3%
E Glu5 · 13%
N Asn1 · 3%
Q Gln1 · 3%
S Ser5 · 13%
T Thr2 · 5%
C Cys0 · 0%
G Gly5 · 13%
P Pro4 · 10%

3D structure

No 3D structure

No experimental structure (PDB) and no UniProt entry for an AlphaFold model are listed for this peptide. Synthetic peptides often have neither. The sequence view above is the reference.

2D structure

Exenatide (exendin-4) has 39 residues. A full-atom drawing is hard to read at this size; the sequence view is the reference.

SMILES fromPubChem CID 45588096(opens in a new tab)

CC[C@H](C)[C@@H](C(=O)N[C@@H](CCC(=O)O)C(=O)N[C@@H](CC1=CNC2=CC=CC=C21)C(=O)N[C@@H](CC(C)C)C(=O)N[C@@H](CCCCN)C(=O)N[C@@H](CC(=O)N)C(=O)NCC(=O)NCC(=O)N3CCC[C@H]3C(=O)N[C@@H](CO)C(=O)N[C@@H](CO)C(=O)NCC(=O)N[C@@H](C)C(=O)N4CCC[C@H]4C(=O)N5CCC[C@H]5C(=O)N6CCC[C@H]6C(=O)N[C@@H](CO)C(=O)N)NC(=O)[C@H](CC7=CC=CC=C7)NC(=O)[C@H](CC(C)C)NC(=O)[C@H](CCCNC(=N)N)NC(=O)[C@H](C(C)C)NC(=O)[C@H](C)NC(=O)[C@H](CCC(=O)O)NC(=O)[C@H](CCC(=O)O)NC(=O)[C@H](CCC(=O)O)NC(=O)[C@H](CCSC)NC(=O)[C@H](CCC(=O)N)NC(=O)[C@H](CCCCN)NC(=O)[C@H](CO)NC(=O)[C@H](CC(C)C)NC(=O)[C@H](CC(=O)O)NC(=O)[C@H](CO)NC(=O)[C@H]([C@@H](C)O)NC(=O)[C@H](CC8=CC=CC=C8)NC(=O)[C@H]([C@@H](C)O)NC(=O)CNC(=O)[C@H](CCC(=O)O)NC(=O)CNC(=O)[C@H](CC9=CNC=N9)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 Exenatide (exendin-4), 39 residues at 100 degrees per residue. Hydrophobic moment 0.19 pointing at 274 degrees.His 1, Eisenberg consensus (normalized) -0.40H1Gly 2, Eisenberg consensus (normalized) 0.48G2Glu 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−9Leu 10, Eisenberg consensus (normalized) 1.06L10Ser 11, Eisenberg consensus (normalized) -0.18S11Lys 12, Eisenberg consensus (normalized) -1.50K+12Gln 13, Eisenberg consensus (normalized) -0.85Q13Met 14, Eisenberg consensus (normalized) 0.64M14Glu 15, Eisenberg consensus (normalized) -0.74E−15Glu 16, Eisenberg consensus (normalized) -0.74E−16Glu 17, Eisenberg consensus (normalized) -0.74E−17Ala 18, Eisenberg consensus (normalized) 0.62A18Val 19, Eisenberg consensus (normalized) 1.08V19Arg 20, Eisenberg consensus (normalized) -2.53R+20Leu 21, Eisenberg consensus (normalized) 1.06L21Phe 22, Eisenberg consensus (normalized) 1.19F22Ile 23, Eisenberg consensus (normalized) 1.38I23Glu 24, Eisenberg consensus (normalized) -0.74E−24Trp 25, Eisenberg consensus (normalized) 0.81W25Leu 26, Eisenberg consensus (normalized) 1.06L26Lys 27, Eisenberg consensus (normalized) -1.50K+27Asn 28, Eisenberg consensus (normalized) -0.78N28Gly 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
0.194
μH, best 11-residue window
0.708
Arrow direction
274°
Residues
39 · 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)
1H0°-0.40
2G100°0.48
3E200°-0.74
4G300°0.48
5T40°-0.05
6F140°1.19
7T240°-0.05
8S340°-0.18
9D80°-0.90
10L180°1.06
11S280°-0.18
12K20°-1.50
13Q120°-0.85
14M220°0.64
15E320°-0.74
16E60°-0.74
17E160°-0.74
18A260°0.62
19V0°1.08
20R100°-2.53
21L200°1.06
22F300°1.19
23I40°1.38
24E140°-0.74
25W240°0.81
26L340°1.06
27K80°-1.50
28N180°-0.78
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