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Pramlintide (Symlin) / Studies
Synthetic analog · 37 amino acids · 3,949 Da

Pramlintide (Symlin) studies and research data

PepBank has 145 pramlintide studies with results. 111 of them gave pramlintide, with 595 results, grouped by what the studies measured. In each group, results from studies in people come first. Data as of 2026-10-30.

Searches 595 results and 456 papers. Newer studies from Europe PMC

Results in people
453
76% of 595 results
Results in animals
85
14% of 595 results
Results in lab cells
57
10% of 595 results
From computer models
0
0% of 595 results
The molecule

Pramlintide identity

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

Pramlintide contains 37 residues and a Cys2-Cys7 disulfide bond. Proline replaces human amylin residues Ala25, Ser28, and Ser29. The C-terminus is amidated. Symlin contains the acetate salt. The query requires pramlintide naming and does not use amylin alone.

Kind
Synthetic analog · 37 residues
Identifiers
UniProtP10997 (opens in a new tab)PubChem CID70691388 (opens in a new tab)UNIID3FM8FA78T (opens in a new tab)DrugBankDB01278 (opens in a new tab)CAS151126-32-8
Parent
Analog of Amylin, human · residues 34-70The label defines three substitutions from mature human amylin. UniProt P10997 marks the mature peptide at residues 34-70.
Development
Approved in the US (Symlin)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
Amylin receptor complexesAgonistoriginal receptor pharmacology studySource (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 · 1 modification · 1 disulfide bond

H-
Residues 1 to 10:
KCNTATCATQ
Residues 11 to 20:
RLANFLVHSS
Residues 21 to 30:
NNFGPILPPT
Residues 31 to 37:
NVGSNTY
  • HydrophobicA V I L M
  • AromaticF W Y
  • PositiveK R H
  • PolarS T N Q
  • SpecialC G P
  • Modified residue
  • Disulfide partner

Modifications

37
C-terminal amide
C-terminal carboxamide.
Cys2–Cys7
Disulfide bond

Alignment to Amylin

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

34 of 37 aligned residues identical (92%) · 3 substitutions · 1 modified residue · Amylin 1–37

  • Top row: Amylin (parent)
  • Bottom row: Pramlintide (Symlin)
KCNTATCATQ
RLANFLVHSS
NNFGILT
NVGSNT
  • Same as parent
  • Substituted
  • Non-canonical or D-form
  • Added
  • Gap
  • Modified side chain or end

Differences from the parent

  1. 1Parent 25 · analog 25Ala → Pro · Substitution
  2. 2Parent 28 · analog 28Ser → Pro · Substitution
  3. 3Parent 29 · analog 29Ser → Pro · Substitution
  4. 4Parent 37 · analog 37Tyr, modified · C-terminal amideC-terminal carboxamide.

Basis: The label defines three substitutions from mature human amylin. UniProt P10997 marks the mature peptide at residues 34-70.

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
C171H267N51O53S2
Molecular weight
3,949 g/mol
Monoisotopic mass
3,946.9207 Da

Calculated from the sequence

Average mass
3,949.43 Da
Sum of ExPASy residue masses + water + C-amide, 1 disulfide · ExPASy Compute pI/Mw; FindMod
Monoisotopic mass
3,946.9207 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)
−0.232
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
9.44
Dipeptide instability weights (DIWV) · Guruprasad et al. 1990
40 or below: classed as stable (ExPASy).
Aliphatic index
65.9
Mole % A + 2.9 V + 3.9 (I + L) · Ikai 1980
Boman index
1.35 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

Net charge of Pramlintide (Symlin) from pH 0 to 14 (EMBOSS pKa set). Isoelectric point 11.70. Net charge at pH 7.4: 3.05.−10+1+2+3+402468101214pHNet chargepH 7.4pI 11.70

Henderson-Hasselbalch, EMBOSS pKa set, C-amide, 1 disulfide. Calculated, not measured.

Show as table
pHNet charge
04.00
14.00
24.00
34.00
44.00
53.97
63.76
73.21
82.82
92.20
101.46
110.47
12−0.17
13−0.75
14−0.97

Composition

  • Hydrophobic24% (9)
  • Aromatic8% (3)
  • Positive8% (3)
  • Polar41% (15)
  • Special19% (7)

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

A Ala3 · 8%
I Ile1 · 3%
L Leu3 · 8%
M Met0 · 0%
V Val2 · 5%
F Phe2 · 5%
W Trp0 · 0%
Y Tyr1 · 3%
H His1 · 3%
K Lys1 · 3%
R Arg1 · 3%
D Asp0 · 0%
E Glu0 · 0%
N Asn6 · 16%
Q Gln1 · 3%
S Ser3 · 8%
T Thr5 · 14%
C Cys2 · 5%
G Gly2 · 5%
P Pro3 · 8%

3D structure

PredictedAlphaFold DB · P10997

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 P10997, not an experimental structure of Pramlintide (Symlin). Pramlintide (Symlin) = residues 34–70.

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

2D structure

Pramlintide (Symlin) has 37 residues. A full-atom drawing is hard to read at this size; the sequence view is the reference.

SMILES fromPubChem CID 70691388(opens in a new tab)

CC[C@H](C)[C@@H](C(=O)N[C@@H](CC(C)C)C(=O)N1CCC[C@H]1C(=O)N2CCC[C@H]2C(=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](CC3=CC=C(C=C3)O)C(=O)N)NC(=O)[C@@H]4CCCN4C(=O)CNC(=O)[C@H](CC5=CC=CC=C5)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](CC6=CNC=N6)NC(=O)[C@H](C(C)C)NC(=O)[C@H](CC(C)C)NC(=O)[C@H](CC7=CC=CC=C7)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]8CSSC[C@@H](C(=O)N[C@H](C(=O)N[C@H](C(=O)N[C@H](C(=O)N[C@H](C(=O)N8)[C@@H](C)O)C)[C@@H](C)O)CC(=O)N)NC(=O)[C@H](CCCCN)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 Pramlintide (Symlin), 37 residues at 100 degrees per residue. Hydrophobic moment 0.20 pointing at 46 degrees.Lys 1, Eisenberg consensus (normalized) -1.50K+1Cys 2, Eisenberg consensus (normalized) 0.29C2Asn 3, Eisenberg consensus (normalized) -0.78N3Thr 4, Eisenberg consensus (normalized) -0.05T4Ala 5, Eisenberg consensus (normalized) 0.62A5Thr 6, Eisenberg consensus (normalized) -0.05T6Cys 7, Eisenberg consensus (normalized) 0.29C7Ala 8, Eisenberg consensus (normalized) 0.62A8Thr 9, Eisenberg consensus (normalized) -0.05T9Gln 10, Eisenberg consensus (normalized) -0.85Q10Arg 11, Eisenberg consensus (normalized) -2.53R+11Leu 12, Eisenberg consensus (normalized) 1.06L12Ala 13, Eisenberg consensus (normalized) 0.62A13Asn 14, Eisenberg consensus (normalized) -0.78N14Phe 15, Eisenberg consensus (normalized) 1.19F15Leu 16, Eisenberg consensus (normalized) 1.06L16Val 17, Eisenberg consensus (normalized) 1.08V17His 18, Eisenberg consensus (normalized) -0.40H18Ser 19, Eisenberg consensus (normalized) -0.18S19Ser 20, Eisenberg consensus (normalized) -0.18S20Asn 21, Eisenberg consensus (normalized) -0.78N21Asn 22, Eisenberg consensus (normalized) -0.78N22Phe 23, Eisenberg consensus (normalized) 1.19F23Gly 24, Eisenberg consensus (normalized) 0.48G24Pro 25, Eisenberg consensus (normalized) 0.12P25Ile 26, Eisenberg consensus (normalized) 1.38I26Leu 27, Eisenberg consensus (normalized) 1.06L27Pro 28, Eisenberg consensus (normalized) 0.12P28Pro 29, Eisenberg consensus (normalized) 0.12P29Thr 30, Eisenberg consensus (normalized) -0.05T30Asn 31, Eisenberg consensus (normalized) -0.78N31Val 32, Eisenberg consensus (normalized) 1.08V32Gly 33, Eisenberg consensus (normalized) 0.48G33Ser 34, Eisenberg consensus (normalized) -0.18S34Asn 35, Eisenberg consensus (normalized) -0.78N35Thr 36, Eisenberg consensus (normalized) -0.05T36Tyr 37, Eisenberg consensus (normalized) 0.26Y37
μH, residues shown
0.201
μH, best 11-residue window
0.484
Arrow direction
46°
Residues
37 · 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)
1K0°-1.50
2C100°0.29
3N200°-0.78
4T300°-0.05
5A40°0.62
6T140°-0.05
7C240°0.29
8A340°0.62
9T80°-0.05
10Q180°-0.85
11R280°-2.53
12L20°1.06
13A120°0.62
14N220°-0.78
15F320°1.19
16L60°1.06
17V160°1.08
18H260°-0.40
19S0°-0.18
20S100°-0.18
21N200°-0.78
22N300°-0.78
23F40°1.19
24G140°0.48
25P240°0.12
26I340°1.38
27L80°1.06
28P180°0.12
29P280°0.12
30T20°-0.05
31N120°-0.78
32V220°1.08
33G320°0.48
34S60°-0.18
35N160°-0.78
36T260°-0.05
37Y0°0.26
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