RecruitingPhase 3NCT07321886
A Study of Eloralintide (LY3841136) in Participants With Obesity, or Overweight Without Type 2 Diabetes
Eli Lilly and Companyn = 1,9806 Feb 2026 to est. Jul 2030
Obesity · Overweight
Eloralintide / Studies
Synthetic analog · 36 amino acids · 4,526 Da
Eloralintide studies and research data
PepBank has no study results for Eloralintide yet. Data as of 2026-10-30.
Searches 0 results and 10 papers. Newer studies from Europe PMC
Results in people
0
0% of 0 results
Results in animals
0
0% of 0 results
Results in lab cells
0
0% of 0 results
From computer models
0
0% of 0 results
The molecule
Eloralintide identity
Identifiers, parent molecule, targets and development stage, from curated data.
Eloralintide is a modified amylin analogue. GSRS records a 36-residue main chain and a separately linked gamma-glutamyl residue. It includes ornithine, alpha-methylphenylalanine, N-methylasparagine, a thioether ring and an acylated lysine. These features distinguish it from amylin, pramlintide and cagrilintide. Lilly lists ENLIGHTEN-1 as a recruiting phase 3 obesity trial. No FDA or EMA marketing approval was found.
- Kind
- Synthetic analog · 36 residues
- Identifiers
- UniProtP10997 (opens in a new tab)PubChem CID175663130 (opens in a new tab)UNII73G3354J8W (opens in a new tab)CAS2883634-40-8
- Parent
- Analog of Amylin, humanLilly and the indexed titles describe an amylin receptor agonist. GSRS defines an extensively modified amylin-like sequence.
- Development
- Phase 3Eli Lilly and CompanyENLIGHTEN-1, NCT07321886, is a recruiting phase 3 trial sponsored by Eli Lilly and Company. The registry describes subcutaneous administration, not an approved label. Source (opens in a new tab)
Targets
| Target | Action | Evidence |
|---|---|---|
| Amylin receptor complexes | Agonist | indexed publication titleSource (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
36 amino acids · 7 modifications
Residues 1 to 10:
NTATCATG
Residues 11 to 20:
LAELVRSSN
Residues 21 to 30:
FGPLPPTE
Residues 31 to 36:
VGSNTY
Alignment to Amylin
Calculated from the two sequences. Curated notes are shown as given.
26 of 36 aligned residues identical (72%) · 8 substitutions · 2 non-canonical residues · 3 modified residues · Amylin 2–37
- Top row: Amylin (parent)
- Bottom row: Eloralintide
NTATCAT
LALVSS
NFGLT
VGSNT
- Same as parent
- Substituted
- Non-canonical or D-form
- Added
- Gap
- Modified side chain or end
- Parent context
Differences from the parent
- 1Parent 2 · analog 1Cys, modified · Other modificationGamma-glutamyl residue is separately linked at the N-terminal cysteine. GSRS records it as a second E subunit.
- 2Parent 10 · analog 9Gln → Gly · Substitution
- 3Parent 11 · analog 10Arg → Xaa · Non-canonical residueL-ornithine. X replaces the GSRS placeholder in sequence.
- 4Parent 14 · analog 13Asn → Glu · Substitution
- 5Parent 15 · analog 14Phe → Xaa · Non-canonical residueL-alpha-methylphenylalanine. X denotes the modified residue.
- 6Parent 18 · analog 17His → Arg · Substitution
- 7Parent 22 · analog 21Asn, modified · Other modificationN-methyl-L-asparagine.
- 8Parent 25 · analog 24Ala → Pro · Substitution
- 9Parent 26 · analog 25Ile → Lys · SubstitutionLys side chain carries a C20 diacid through two gamma-glutamyl linkers.
- 10Parent 28 · analog 27Ser → Pro · Substitution
- 11Parent 29 · analog 28Ser → Pro · Substitution
- 12Parent 31 · analog 30Asn → Glu · Substitution
- 13Parent 37 · analog 36Tyr, modified · C-terminal amideC-terminal L-tyrosinamide.
Basis: Lilly and the indexed titles describe an amylin receptor agonist. GSRS defines an extensively modified amylin-like sequence.
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
- C201H319N49O65S2
- Molecular weight
- 4,526 g/mol
- Monoisotopic mass
- 4,523.2604 Da
- PubChem CID 175663130(opens in a new tab)retrieved 2026-10-21
- GSRS UNII 73G3354J8W(opens in a new tab)retrieved 2026-10-21
Calculated from the sequence
Some values cannot be calculated. The sequence has a non-canonical residue (X). Residue tables cover only the 20 standard amino acids.
- Average mass
- Not calculated
- Monoisotopic mass
- Not calculated
- Isoelectric point (pI)
- Not calculated
- Net charge at pH 7.4
- Not calculated
- GRAVY (hydropathy)
- Not calculated
- 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
- Not calculated
- Aliphatic index
- Not calculated
- Boman index
- Not calculated
- Hydrophobic moment (μH)
- Not calculated
- 2 non-canonical residues (X) are not included in calculated values.
- Not included: other modification, lipid chain. Mass, charge and pI are not calculated; use the identity-source values.
- The N-terminal group is not modeled.
- 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
No charge curve
The sequence has a non-canonical residue (X). Residue tables cover only the 20 standard amino acids.
Composition
- Hydrophobic22% (8)A L V
- Aromatic6% (2)F Y
- Positive6% (2)K R
- Negative6% (2)E
- Polar33% (12)N S T
- Special22% (8)C G P
- Non-canonical6% (2)X
36 residues. Each residue counts in one class; F and W count as aromatic.
A Ala3 · 8%
I Ile0 · 0%
L Leu3 · 8%
M Met0 · 0%
V Val2 · 6%
F Phe1 · 3%
W Trp0 · 0%
Y Tyr1 · 3%
H His0 · 0%
K Lys1 · 3%
R Arg1 · 3%
D Asp0 · 0%
E Glu2 · 6%
N Asn4 · 11%
Q Gln0 · 0%
S Ser3 · 8%
T Thr5 · 14%
C Cys2 · 6%
G Gly3 · 8%
P Pro3 · 8%
X Xaa2 · 6%
3D structure
PredictedAlphaFold DB · P10997
Loads the 3D viewer (3Dmol.js, about 150 KB) and the model file from AlphaFold DB (EMBL-EBI).
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.
- μH, residues shown
- 0.211
- μH, best 11-residue window
- —
- Arrow direction
- 330°
- Residues
- 36 · 2 rings of 18 · 2 X not scored
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
| Position | Residue | Angle | Eisenberg consensus (normalized) |
|---|---|---|---|
| 1 | C | 0° | 0.29 |
| 2 | N | 100° | -0.78 |
| 3 | T | 200° | -0.05 |
| 4 | A | 300° | 0.62 |
| 5 | T | 40° | -0.05 |
| 6 | C | 140° | 0.29 |
| 7 | A | 240° | 0.62 |
| 8 | T | 340° | -0.05 |
| 9 | G | 80° | 0.48 |
| 10 | X | 180° | not scored |
| 11 | L | 280° | 1.06 |
| 12 | A | 20° | 0.62 |
| 13 | E | 120° | -0.74 |
| 14 | X | 220° | not scored |
| 15 | L | 320° | 1.06 |
| 16 | V | 60° | 1.08 |
| 17 | R | 160° | -2.53 |
| 18 | S | 260° | -0.18 |
| 19 | S | 0° | -0.18 |
| 20 | N | 100° | -0.78 |
| 21 | N | 200° | -0.78 |
| 22 | F | 300° | 1.19 |
| 23 | G | 40° | 0.48 |
| 24 | P | 140° | 0.12 |
| 25 | K | 240° | -1.50 |
| 26 | L | 340° | 1.06 |
| 27 | P | 80° | 0.12 |
| 28 | P | 180° | 0.12 |
| 29 | T | 280° | -0.05 |
| 30 | E | 20° | -0.74 |
| 31 | V | 120° | 1.08 |
| 32 | G | 220° | 0.48 |
| 33 | S | 320° | -0.18 |
| 34 | N | 60° | -0.78 |
| 35 | T | 160° | -0.05 |
| 36 | Y | 260° | 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.
No study of Eloralintide has results in PepBank yet.
Trials and papers
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.
Eloralintide studies: 0 papers with results
No paper with results is linked to this peptide.
Status and safety
Data