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Cosyntropin / Studies
Natural fragment · 24 amino acids · 2,933.4 Da

Cosyntropin studies and research data

PepBank has 57 cosyntropin studies with results. 28 of them gave cosyntropin, with 97 results, grouped by what the studies measured. In each group, results from studies in people come first. Data as of 2026-10-30.

Searches 97 results and 992 papers. Newer studies from Europe PMC

Results in people
70
72% of 97 results
Results in animals
25
26% of 97 results
Results in lab cells
2
2% of 97 results
From computer models
0
0% of 97 results
The molecule

Cosyntropin identity

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

Cosyntropin, or tetracosactide, matches the first 24 residues of ACTH. The cited US label uses it as a diagnostic agent for adrenocortical insufficiency.

Kind
Natural fragment · 24 residues
Identifiers
ChEMBLCHEMBL2103784 (opens in a new tab)PubChem CID16133751 (opens in a new tab)UNII72YY86EA29 (opens in a new tab)DrugBankDB01284 (opens in a new tab)CAS16960-16-0
Parent
Fragment of Corticotropin · residues 138-161UniProt P01189 places mature human corticotropin at residues 138-176. Cosyntropin equals precursor residues 138-161 and mature corticotropin residues 1-24. This parent denotes the pure sequence, not the Acthar mixture.
Development
Approved in the US (Cortrosyn)An approved medicinal product exists. Availability and other indications can differ. Source (opens in a new tab)

Targets

Molecular targets with action and evidence source
TargetActionEvidence
Melanocortin 2 receptorMC2RQ01718 (opens in a new tab)AgonistOpen Targets mechanism table, curated from ChEMBLSource (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

24 amino acids

H-
Residues 1 to 10:
SYSMEHFRWG
Residues 11 to 20:
KPVGKKRRPV
Residues 21 to 24:
KVYP
-OH
  • HydrophobicA V I L M
  • AromaticF W Y
  • PositiveK R H
  • NegativeD E
  • PolarS T N Q
  • SpecialC G P

Alignment to Corticotropin

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

24 of 24 aligned residues identical (100%) · Corticotropin 1–24

  • Top row: Corticotropin (parent)
  • Bottom row: Cosyntropin
SYSMEHFRWG
KPVGKKRRPV
KVYP
  • Same as parent
  • Substituted
  • Non-canonical or D-form
  • Added
  • Gap
  • Modified side chain or end
  • Parent context

No differences in the aligned region.

Basis: UniProt P01189 places mature human corticotropin at residues 138-176. Cosyntropin equals precursor residues 138-161 and mature corticotropin residues 1-24. This parent denotes the pure sequence, not the Acthar mixture.

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
C136H210N40O31S
Molecular weight
2,933.4 g/mol
Monoisotopic mass
2,931.5806 Da

Calculated from the sequence

Average mass
2,933.47 Da
Sum of ExPASy residue masses + water · ExPASy Compute pI/Mw; FindMod
Monoisotopic mass
2,931.5806 Da
Sum of ExPASy residue masses + water · ExPASy FindMod
Isoelectric point (pI)
11.26
pH of zero net charge, EMBOSS pKa set · EMBOSS iep, Epk.dat
Net charge at pH 7.4
6.05
Henderson-Hasselbalch, EMBOSS pKa set · EMBOSS iep, Epk.dat
GRAVY (hydropathy)
−1.217
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
66.70
Dipeptide instability weights (DIWV) · Guruprasad et al. 1990
Above 40: classed as possibly unstable (ExPASy).
Aliphatic index
36.3
Mole % A + 2.9 V + 3.9 (I + L) · Ikai 1980
Boman index
2.66 kcal/mol
Mean solubility value (negated) · Boman 2003
Above 2.48: high protein-binding potential (Boman).
Hydrophobic moment (μH)
0.592
Eisenberg scale, 100° per residue, best 11-residue window · Eisenberg et al. 1982, 1984
pI with each pKa set
EMBOSS 11.26Bjellqvist (ExPASy) 10.64IPC peptide 11.06IPC protein 10.74
  • 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 11.26 · Net charge at pH 7.4: 6.05

Point or use arrow keys

Net charge of Cosyntropin from pH 0 to 14 (EMBOSS pKa set). Isoelectric point 11.26. Net charge at pH 7.4: 6.05.−50+5+1002468101214pHNet chargepH 7.4pI 11.26

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

Show as table
pHNet charge
09.00
19.00
28.97
38.73
47.84
57.12
66.77
76.22
85.81
95.08
103.60
110.68
12−1.46
13−3.25
14−3.91

Composition

  • Hydrophobic17% (4)
  • Aromatic17% (4)
  • Positive33% (8)
  • Negative4% (1)
  • Polar8% (2)
  • Special21% (5)

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

A Ala0 · 0%
I Ile0 · 0%
L Leu0 · 0%
M Met1 · 4%
V Val3 · 13%
F Phe1 · 4%
W Trp1 · 4%
Y Tyr2 · 8%
H His1 · 4%
K Lys4 · 17%
R Arg3 · 13%
D Asp0 · 0%
E Glu1 · 4%
N Asn0 · 0%
Q Gln0 · 0%
S Ser2 · 8%
T Thr0 · 0%
C Cys0 · 0%
G Gly2 · 8%
P Pro3 · 13%

3D structure

PredictedAlphaFold DB · P01189

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 P01189, not an experimental structure of Cosyntropin. Cosyntropin = residues 138–161.

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

2D structure

Cosyntropin has 24 residues. A full-atom drawing is hard to read at this size; the sequence view is the reference.

SMILES fromPubChem CID 16133751(opens in a new tab)

CC(C)[C@@H](C(=O)NCC(=O)N[C@@H](CCCCN)C(=O)N[C@@H](CCCCN)C(=O)N[C@@H](CCCNC(=N)N)C(=O)N[C@@H](CCCNC(=N)N)C(=O)N1CCC[C@H]1C(=O)N[C@@H](C(C)C)C(=O)N[C@@H](CCCCN)C(=O)N[C@@H](C(C)C)C(=O)N[C@@H](CC2=CC=C(C=C2)O)C(=O)N3CCC[C@H]3C(=O)O)NC(=O)[C@@H]4CCCN4C(=O)[C@H](CCCCN)NC(=O)CNC(=O)[C@H](CC5=CNC6=CC=CC=C65)NC(=O)[C@H](CCCNC(=N)N)NC(=O)[C@H](CC7=CC=CC=C7)NC(=O)[C@H](CC8=CN=CN8)NC(=O)[C@H](CCC(=O)O)NC(=O)[C@H](CCSC)NC(=O)[C@H](CO)NC(=O)[C@H](CC9=CC=C(C=C9)O)NC(=O)[C@H](CO)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 Cosyntropin, 24 residues at 100 degrees per residue. Hydrophobic moment 0.18 pointing at 110 degrees.Ser 1, Eisenberg consensus (normalized) -0.18S1Tyr 2, Eisenberg consensus (normalized) 0.26Y2Ser 3, Eisenberg consensus (normalized) -0.18S3Met 4, Eisenberg consensus (normalized) 0.64M4Glu 5, Eisenberg consensus (normalized) -0.74E−5His 6, Eisenberg consensus (normalized) -0.40H6Phe 7, Eisenberg consensus (normalized) 1.19F7Arg 8, Eisenberg consensus (normalized) -2.53R+8Trp 9, Eisenberg consensus (normalized) 0.81W9Gly 10, Eisenberg consensus (normalized) 0.48G10Lys 11, Eisenberg consensus (normalized) -1.50K+11Pro 12, Eisenberg consensus (normalized) 0.12P12Val 13, Eisenberg consensus (normalized) 1.08V13Gly 14, Eisenberg consensus (normalized) 0.48G14Lys 15, Eisenberg consensus (normalized) -1.50K+15Lys 16, Eisenberg consensus (normalized) -1.50K+16Arg 17, Eisenberg consensus (normalized) -2.53R+17Arg 18, Eisenberg consensus (normalized) -2.53R+18Pro 19, Eisenberg consensus (normalized) 0.12P19Val 20, Eisenberg consensus (normalized) 1.08V20Lys 21, Eisenberg consensus (normalized) -1.50K+21Val 22, Eisenberg consensus (normalized) 1.08V22Tyr 23, Eisenberg consensus (normalized) 0.26Y23Pro 24, Eisenberg consensus (normalized) 0.12P24
μH, residues shown
0.177
μH, best 11-residue window
0.592
Arrow direction
110°
Residues
24 · 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)
1S0°-0.18
2Y100°0.26
3S200°-0.18
4M300°0.64
5E40°-0.74
6H140°-0.40
7F240°1.19
8R340°-2.53
9W80°0.81
10G180°0.48
11K280°-1.50
12P20°0.12
13V120°1.08
14G220°0.48
15K320°-1.50
16K60°-1.50
17R160°-2.53
18R260°-2.53
19P0°0.12
20V100°1.08
21K200°-1.50
22V300°1.08
23Y40°0.26
24P140°0.12
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