Skip to content
Glucagon / Studies
Natural peptide · 29 amino acids · 3,482.8 Da

Glucagon studies and research data

PepBank has 128 glucagon studies with results. 119 of them gave glucagon, with 627 results, grouped by what the studies measured. In each group, results from studies in people come first. Data as of 2026-10-30.

Searches 627 results and 614 papers. Newer studies from Europe PMC

Results in people
518
83% of 627 results
Results in animals
109
17% of 627 results
Results in lab cells
0
0% of 627 results
From computer models
0
0% of 627 results
The molecule

Glucagon identity

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

This existing record covers the 29-residue human glucagon sequence and its medicinal formulations. Glucagon treats severe hypoglycemia and has diagnostic uses. Glucagon analogs and GLP-1 drugs have separate records.

Kind
Natural peptide · 29 residues
Identifiers
UniProtP01275 (opens in a new tab)ChEMBLCHEMBL5314341 (opens in a new tab)PubChem CID16132283 (opens in a new tab)UNII76LA80IG2G (opens in a new tab)DrugBankDB00040 (opens in a new tab)CAS16941-32-5KEGGD00116 (opens in a new tab)IUPHAR1136 (opens in a new tab)
Development
Approved in the US and EU (GlucaGen, 1998)Several manufacturers. First FDA application NDA012122 (Eli Lilly), original approval 1960-11-14. Source (opens in a new tab)

Targets

Molecular targets with action and evidence source
TargetActionEvidence
Glucagon receptorGCGRP47871 (opens in a new tab)Agonistprimary literatureSource (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

29 amino acids

H-
Residues 1 to 10:
HSQGTFTSDY
Residues 11 to 20:
SKYLDSRRAQ
Residues 21 to 29:
DFVQWLMNT
-OH
  • HydrophobicA V I L M
  • AromaticF W Y
  • PositiveK R H
  • NegativeD E
  • PolarS T N Q
  • SpecialC G P

Properties

From identity sources

Formula
C153H225N43O49S
Molecular weight
3,482.75 g/mol
Monoisotopic mass
3,480.6157 Da

Calculated from the sequence

Average mass
3,482.79 Da
Sum of ExPASy residue masses + water · ExPASy Compute pI/Mw; FindMod
Monoisotopic mass
3,480.6157 Da
Sum of ExPASy residue masses + water · ExPASy FindMod
Isoelectric point (pI)
7.54
pH of zero net charge, EMBOSS pKa set · EMBOSS iep, Epk.dat
Net charge at pH 7.4
0.05
Henderson-Hasselbalch, EMBOSS pKa set · EMBOSS iep, Epk.dat
GRAVY (hydropathy)
−0.990
Mean Kyte-Doolittle hydropathy · Kyte and Doolittle 1982
Negative: hydrophilic on average.
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
56.03
Dipeptide instability weights (DIWV) · Guruprasad et al. 1990
Above 40: classed as possibly unstable (ExPASy).
Aliphatic index
40.3
Mole % A + 2.9 V + 3.9 (I + L) · Ikai 1980
Boman index
2.89 kcal/mol
Mean solubility value (negated) · Boman 2003
Above 2.48: high protein-binding potential (Boman).
Hydrophobic moment (μH)
0.655
Eisenberg scale, 100° per residue, best 11-residue window · Eisenberg et al. 1982, 1984
pI with each pKa set
EMBOSS 7.54Bjellqvist (ExPASy) 6.75IPC peptide 7.67IPC protein 7.21
  • 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 7.54 · Net charge at pH 7.4: 0.05

Point or use arrow keys

Net charge of Glucagon from pH 0 to 14 (EMBOSS pKa set). Isoelectric point 7.54. Net charge at pH 7.4: 0.05.−10−50+502468101214pHNet chargepH 7.4pI 7.54

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

Show as table
pHNet charge
05.00
14.99
24.94
34.46
42.61
51.23
60.78
70.22
8−0.19
9−0.88
10−1.99
11−3.45
12−4.40
13−5.51
14−5.94

Composition

  • Hydrophobic17% (5)
  • Aromatic17% (5)
  • Positive14% (4)
  • Negative10% (3)
  • Polar38% (11)
  • Special3% (1)

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

A Ala1 · 3%
I Ile0 · 0%
L Leu2 · 7%
M Met1 · 3%
V Val1 · 3%
F Phe2 · 7%
W Trp1 · 3%
Y Tyr2 · 7%
H His1 · 3%
K Lys1 · 3%
R Arg2 · 7%
D Asp3 · 10%
E Glu0 · 0%
N Asn1 · 3%
Q Gln3 · 10%
S Ser4 · 14%
T Thr3 · 10%
C Cys0 · 0%
G Gly1 · 3%
P Pro0 · 0%

3D structure

PredictedAlphaFold DB · P01275

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 P01275, not an experimental structure of Glucagon.

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

2D structure

Glucagon has 29 residues. A full-atom drawing is hard to read at this size; the sequence view is the reference.

SMILES fromPubChem CID 16132283(opens in a new tab)

C[C@H]([C@@H](C(=O)N[C@@H](CC1=CC=CC=C1)C(=O)N[C@@H]([C@@H](C)O)C(=O)N[C@@H](CO)C(=O)N[C@@H](CC(=O)O)C(=O)N[C@@H](CC2=CC=C(C=C2)O)C(=O)N[C@@H](CO)C(=O)N[C@@H](CCCCN)C(=O)N[C@@H](CC3=CC=C(C=C3)O)C(=O)N[C@@H](CC(C)C)C(=O)N[C@@H](CC(=O)O)C(=O)N[C@@H](CO)C(=O)N[C@@H](CCCNC(=N)N)C(=O)N[C@@H](CCCNC(=N)N)C(=O)N[C@@H](C)C(=O)N[C@@H](CCC(=O)N)C(=O)N[C@@H](CC(=O)O)C(=O)N[C@@H](CC4=CC=CC=C4)C(=O)N[C@@H](C(C)C)C(=O)N[C@@H](CCC(=O)N)C(=O)N[C@@H](CC5=CNC6=CC=CC=C65)C(=O)N[C@@H](CC(C)C)C(=O)N[C@@H](CCSC)C(=O)N[C@@H](CC(=O)N)C(=O)N[C@@H]([C@@H](C)O)C(=O)O)NC(=O)CNC(=O)[C@H](CCC(=O)N)NC(=O)[C@H](CO)NC(=O)[C@H](CC7=CN=CN7)N)O

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 Glucagon, 29 residues at 100 degrees per residue. Hydrophobic moment 0.14 pointing at 347 degrees.His 1, Eisenberg consensus (normalized) -0.40H1Ser 2, Eisenberg consensus (normalized) -0.18S2Gln 3, Eisenberg consensus (normalized) -0.85Q3Gly 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) -0.18S11Lys 12, Eisenberg consensus (normalized) -1.50K+12Tyr 13, Eisenberg consensus (normalized) 0.26Y13Leu 14, Eisenberg consensus (normalized) 1.06L14Asp 15, Eisenberg consensus (normalized) -0.90D−15Ser 16, Eisenberg consensus (normalized) -0.18S16Arg 17, Eisenberg consensus (normalized) -2.53R+17Arg 18, Eisenberg consensus (normalized) -2.53R+18Ala 19, Eisenberg consensus (normalized) 0.62A19Gln 20, Eisenberg consensus (normalized) -0.85Q20Asp 21, Eisenberg consensus (normalized) -0.90D−21Phe 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) 1.06L26Met 27, Eisenberg consensus (normalized) 0.64M27Asn 28, Eisenberg consensus (normalized) -0.78N28Thr 29, Eisenberg consensus (normalized) -0.05T29
μH, residues shown
0.140
μH, best 11-residue window
0.655
Arrow direction
347°
Residues
29 · 2 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
2S100°-0.18
3Q200°-0.85
4G300°0.48
5T40°-0.05
6F140°1.19
7T240°-0.05
8S340°-0.18
9D80°-0.90
10Y180°0.26
11S280°-0.18
12K20°-1.50
13Y120°0.26
14L220°1.06
15D320°-0.90
16S60°-0.18
17R160°-2.53
18R260°-2.53
19A0°0.62
20Q100°-0.85
21D200°-0.90
22F300°1.19
23V40°1.08
24Q140°-0.85
25W240°0.81
26L340°1.06
27M80°0.64
28N180°-0.78
29T280°-0.05
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