Amylin, human (islet amyloid polypeptide) studies and research data
PepBank has no study results for Amylin, human (islet amyloid polypeptide) yet. Data as of 2026-10-30.
Searches 0 results and 0 papers. Newer studies from Europe PMC
Amylin, human (islet amyloid polypeptide) identity
Identifiers, parent molecule, targets and development stage, from curated data.
Human amylin (islet amyloid polypeptide, IAPP) is a 37-residue peptide cut from its precursor (UniProt P10997, residues 34-70), with a Cys2-Cys7 disulfide and a C-terminal tyrosine amide. UniProt describes it as a glucoregulatory hormone that acts through amylin receptors (the calcitonin receptor with RAMP1, 2 or 3) and can also bind the calcitonin receptor alone. The synthetic peptide has the INN amlintide (ChEMBL max_phase 2) and is not approved in the US or EU; pramlintide and cagrilintide are amylin analogues.
- Kind
- Natural peptide · 37 residues
- Identifiers
- UniProtP10997 (opens in a new tab)ChEMBLCHEMBL2109025 (opens in a new tab)PubChem CID16132430 (opens in a new tab)UNIIU3U3114NE1 (opens in a new tab)CAS122384-88-7KEGGD02913 (opens in a new tab)
- Development
- Phase 2Synthetic human amylin (amlintide, code AC-001): ChEMBL CHEMBL2109025 max_phase 2. Not approved. Source (opens in a new tab)
Targets
| Target | Action | Evidence |
|---|---|---|
| Amylin receptors (CALCR + RAMP1, RAMP2 or RAMP3)CALCR/RAMP1-3P30988 (opens in a new tab) | Agonist | primary literatureSource (opens in a new tab) |
| Calcitonin receptorCALCRP30988 (opens in a new tab) | Agonist | primary 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
37 amino acids · 2 modifications · 1 disulfide bond
Properties
From identity sources
- Formula
- C165H261N51O55S2
- Molecular weight
- 3,903.28 g/mol
- Monoisotopic mass
- 3,900.8636 Da
- UniProt P10997(opens in a new tab)retrieved 2026-10-08
- GSRS UNII U3U3114NE1(opens in a new tab)retrieved 2026-10-08
- PubChem CID 16132430(opens in a new tab)retrieved 2026-10-08
- Curated KEGG D02913(opens in a new tab)retrieved 2026-10-08
- ChEMBL CHEMBL2109025(opens in a new tab)retrieved 2026-10-08
Calculated from the sequence
- Average mass
- 3,903.32 Da
- Sum of ExPASy residue masses + water + C-amide, 1 disulfide · ExPASy Compute pI/Mw; FindMod
- Monoisotopic mass
- 3,900.8636 Da
- Sum of ExPASy residue masses + water + C-amide, 1 disulfide · ExPASy FindMod
- Isoelectric point (pI)
- 11.70
- pH of zero net charge, EMBOSS pKa set · EMBOSS iep, Epk.dat
- Net charge at pH 7.4
- 3.05
- Henderson-Hasselbalch, EMBOSS pKa set · EMBOSS iep, Epk.dat
- GRAVY (hydropathy)
- −0.097
- Mean Kyte-Doolittle hydropathy · Kyte and Doolittle 1982
- Negative: hydrophilic on average.
- Extinction coefficient, 280 nm (Cys reduced)
- 1,490 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.
- Extinction coefficient, 280 nm (all Cys as cystines)
- 1,615 M⁻¹ cm⁻¹
- 5500 x Trp + 1490 x Tyr + 125 x cystine · Pace et al. 1995 (ExPASy ProtParam)
- Instability index
- 1.94
- Dipeptide instability weights (DIWV) · Guruprasad et al. 1990
- 40 or below: classed as stable (ExPASy).
- Aliphatic index
- 68.6
- Mole % A + 2.9 V + 3.9 (I + L) · Ikai 1980
- Boman index
- 1.49 kcal/mol
- Mean solubility value (negated) · Boman 2003
- 2.48 or below: lower protein-binding potential (Boman).
- Hydrophobic moment (μH)
- 0.484
- Eisenberg scale, 100° per residue, best 11-residue window · Eisenberg et al. 1982, 1984
- pI with each pKa set
- EMBOSS 11.70Bjellqvist (ExPASy) 11.17IPC peptide 11.61IPC protein 11.36
- 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 11.70 · Net charge at pH 7.4: 3.05
Point or use arrow keys
Henderson-Hasselbalch, EMBOSS pKa set, C-amide, 1 disulfide. Calculated, not measured.
Show as table
| pH | Net charge |
|---|---|
| 0 | 4.00 |
| 1 | 4.00 |
| 2 | 4.00 |
| 3 | 4.00 |
| 4 | 4.00 |
| 5 | 3.97 |
| 6 | 3.76 |
| 7 | 3.21 |
| 8 | 2.82 |
| 9 | 2.20 |
| 10 | 1.46 |
| 11 | 0.47 |
| 12 | −0.17 |
| 13 | −0.75 |
| 14 | −0.97 |
Composition
- Hydrophobic27% (10)A I L V
- Aromatic8% (3)F Y
- Positive8% (3)H K R
- Polar46% (17)N Q S T
- Special11% (4)C G
37 residues. Each residue counts in one class; F and W count as aromatic.
3D structure
Loads the 3D viewer (3Dmol.js, about 150 KB) and the model file from AlphaFold DB (EMBL-EBI).
2D structure
Amylin, human (islet amyloid polypeptide) has 37 residues. A full-atom drawing is hard to read at this size; the sequence view is the reference.
SMILES fromPubChem CID 16132430(opens in a new tab)
CC[C@H](C)[C@@H](C(=O)N[C@@H](CC(C)C)C(=O)N[C@@H](CO)C(=O)N[C@@H](CO)C(=O)N[C@@H]([C@@H](C)O)C(=O)N[C@@H](CC(=O)N)C(=O)N[C@@H](C(C)C)C(=O)NCC(=O)N[C@@H](CO)C(=O)N[C@@H](CC(=O)N)C(=O)N[C@@H]([C@@H](C)O)C(=O)N[C@@H](CC1=CC=C(C=C1)O)C(=O)N)NC(=O)[C@H](C)NC(=O)CNC(=O)[C@H](CC2=CC=CC=C2)NC(=O)[C@H](CC(=O)N)NC(=O)[C@H](CC(=O)N)NC(=O)[C@H](CO)NC(=O)[C@H](CO)NC(=O)[C@H](CC3=CN=CN3)NC(=O)[C@H](C(C)C)NC(=O)[C@H](CC(C)C)NC(=O)[C@H](CC4=CC=CC=C4)NC(=O)[C@H](CC(=O)N)NC(=O)[C@H](C)NC(=O)[C@H](CC(C)C)NC(=O)[C@H](CCCNC(=N)N)NC(=O)[C@H](CCC(=O)N)NC(=O)[C@H]([C@@H](C)O)NC(=O)[C@H](C)NC(=O)[C@@H]5CSSC[C@@H](C(=O)N[C@H](C(=O)N[C@H](C(=O)N[C@H](C(=O)N[C@H](C(=O)N5)[C@@H](C)O)C)[C@@H](C)O)CC(=O)N)NC(=O)[C@H](CCCCN)NHelical 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.
- μH, residues shown
- 0.198
- μH, best 11-residue window
- 0.484
- Arrow direction
- 46°
- Residues
- 37 · 3 rings of 18
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
| Position | Residue | Angle | Eisenberg consensus (normalized) |
|---|---|---|---|
| 1 | K | 0° | -1.50 |
| 2 | C | 100° | 0.29 |
| 3 | N | 200° | -0.78 |
| 4 | T | 300° | -0.05 |
| 5 | A | 40° | 0.62 |
| 6 | T | 140° | -0.05 |
| 7 | C | 240° | 0.29 |
| 8 | A | 340° | 0.62 |
| 9 | T | 80° | -0.05 |
| 10 | Q | 180° | -0.85 |
| 11 | R | 280° | -2.53 |
| 12 | L | 20° | 1.06 |
| 13 | A | 120° | 0.62 |
| 14 | N | 220° | -0.78 |
| 15 | F | 320° | 1.19 |
| 16 | L | 60° | 1.06 |
| 17 | V | 160° | 1.08 |
| 18 | H | 260° | -0.40 |
| 19 | S | 0° | -0.18 |
| 20 | S | 100° | -0.18 |
| 21 | N | 200° | -0.78 |
| 22 | N | 300° | -0.78 |
| 23 | F | 40° | 1.19 |
| 24 | G | 140° | 0.48 |
| 25 | A | 240° | 0.62 |
| 26 | I | 340° | 1.38 |
| 27 | L | 80° | 1.06 |
| 28 | S | 180° | -0.18 |
| 29 | S | 280° | -0.18 |
| 30 | T | 20° | -0.05 |
| 31 | N | 120° | -0.78 |
| 32 | V | 220° | 1.08 |
| 33 | G | 320° | 0.48 |
| 34 | S | 60° | -0.18 |
| 35 | N | 160° | -0.78 |
| 36 | T | 260° | -0.05 |
| 37 | Y | 0° | 0.26 |
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.
Newer studies
PepBank reads each paper before it shows the results. This search looks in Europe PMC for newer papers that PepBank has not read yet.
Amylin, human (islet amyloid polypeptide) studies: 0 papers with results
No paper with results is linked to this peptide.