RecruitingPhase 3NCT07795164
Phase 3 Study of the Efficacy, Safety, and Clinical Outcomes of Pemvidutide in MASH
Altimmune, Inc.n = 1,80030 Jul 2026 to est. Dec 2032
Metabolic Dysfunction-Associated Steatohepatitis (MASH)
Pemvidutide / Studies
Conjugate · 29 amino acids
Pemvidutide studies and research data
PepBank has 5 pemvidutide studies with results. 4 of them gave pemvidutide, with 43 results, grouped by what the studies measured. In each group, results from studies in people come first. Data as of 2026-10-30.
Searches 43 results and 17 papers. Newer studies from Europe PMC
Results in people
26
60% of 43 results
Results in animals
17
40% of 43 results
Results in lab cells
0
0% of 43 results
From computer models
0
0% of 43 results
The molecule
Pemvidutide identity
Identifiers, parent molecule, targets and development stage, from curated data.
Pemvidutide is a 29-residue GLP-1 and glucagon receptor dual agonist with a glycolipid conjugate and a Glu16–Lys20 lactam bridge. The code ALT-801 also names an unrelated oncology fusion protein.
- Kind
- Conjugate · 29 residues
- Identifiers
- ChEMBLCHEMBL5095142 (opens in a new tab)UNIIA35F525WBG (opens in a new tab)DrugBankDB18998 (opens in a new tab)CAS2538014-94-5KEGGD12861 (opens in a new tab)
- Development
- Phase 3AltimmuneAltimmune develops pemvidutide. The registry lists a recruiting Phase 3 trial with estimated enrollment. Two completed trials independently establish product eligibility. Registry enrollment includes control groups and does not equal the number who received pemvidutide. Source (opens in a new tab)
Targets
| Target | Action | Evidence |
|---|---|---|
| GLP1RGLP1RP43220 (opens in a new tab) | Agonist | Primary identity or pharmacology sourceSource (opens in a new tab) |
| GCGRGCGRP47871 (opens in a new tab) | Agonist | Primary identity or pharmacology sourceSource (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 · 4 modifications
H-
Residues 1 to 10:
HQGTFTSDY
Residues 11 to 20:
SKYLDAAK
Residues 21 to 29:
EFIQWLLQT
Properties
From identity sources
No formula or molecular weight is listed for Pemvidutide.
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)
- 8,480 M⁻¹ cm⁻¹
- 5500 x Trp + 1490 x Tyr · Pace et al. 1995 (ExPASy ProtParam)
- Instability index
- Not calculated
- Aliphatic index
- Not calculated
- Boman index
- Not calculated
- Hydrophobic moment (μH)
- Not calculated
- 1 non-canonical residue (X) is not included in calculated values.
- Not included: lipid chain. Mass, charge and pI are not calculated; use the identity-source values.
- 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
- Hydrophobic21% (6)A I L
- Aromatic17% (5)F W Y
- Positive14% (4)H K
- Negative14% (4)D E
- Polar28% (8)Q S T
- Special3% (1)G
- Non-canonical3% (1)X
29 residues. Each residue counts in one class; F and W count as aromatic.
A Ala2 · 7%
I Ile1 · 3%
L Leu3 · 10%
M Met0 · 0%
V Val0 · 0%
F Phe2 · 7%
W Trp1 · 3%
Y Tyr2 · 7%
H His1 · 3%
K Lys3 · 10%
R Arg0 · 0%
D Asp2 · 7%
E Glu2 · 7%
N Asn0 · 0%
Q Gln3 · 10%
S Ser2 · 7%
T Thr3 · 10%
C Cys0 · 0%
G Gly1 · 3%
P Pro0 · 0%
X Xaa1 · 3%
3D structure
No 3D structure
No experimental structure (PDB) and no UniProt entry for an AlphaFold model are listed for this peptide. Synthetic peptides often have neither. The sequence view above is the reference.
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
- 0.169
- μH, best 11-residue window
- —
- Arrow direction
- 302°
- Residues
- 29 · 2 rings of 18 · 1 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 | H | 0° | -0.40 |
| 2 | X | 100° | not scored |
| 3 | Q | 200° | -0.85 |
| 4 | G | 300° | 0.48 |
| 5 | T | 40° | -0.05 |
| 6 | F | 140° | 1.19 |
| 7 | T | 240° | -0.05 |
| 8 | S | 340° | -0.18 |
| 9 | D | 80° | -0.90 |
| 10 | Y | 180° | 0.26 |
| 11 | S | 280° | -0.18 |
| 12 | K | 20° | -1.50 |
| 13 | Y | 120° | 0.26 |
| 14 | L | 220° | 1.06 |
| 15 | D | 320° | -0.90 |
| 16 | E | 60° | -0.74 |
| 17 | K | 160° | -1.50 |
| 18 | A | 260° | 0.62 |
| 19 | A | 0° | 0.62 |
| 20 | K | 100° | -1.50 |
| 21 | E | 200° | -0.74 |
| 22 | F | 300° | 1.19 |
| 23 | I | 40° | 1.38 |
| 24 | Q | 140° | -0.85 |
| 25 | W | 240° | 0.81 |
| 26 | L | 340° | 1.06 |
| 27 | L | 80° | 1.06 |
| 28 | Q | 180° | -0.85 |
| 29 | T | 280° | -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
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.
Status and safety
Data