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Amycretin / Studies
Synthetic analog · 68 amino acids · 7,846.7 Da

Amycretin studies and research data

PepBank has 6 amycretin studies with results. 5 of them gave amycretin, with 30 results, grouped by what the studies measured. In each group, results from studies in people come first. Data as of 2026-10-30.

Searches 30 results and 24 papers. Newer studies from Europe PMC

Results in people
21
70% of 30 results
Results in animals
6
20% of 30 results
Results in lab cells
3
10% of 30 results
From computer models
0
0% of 30 results
The molecule

Amycretin identity

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

Amycretin, now also called zenagamtide, is a unimolecular peptide with GLP-1 and amylin receptor agonist moieties. A peptide linker joins the moieties. Its design differs from a mixture of separate GLP-1 and amylin drugs.

Kind
Synthetic analog · 68 residues
Identifiers
UNIIT2EA5S9XJ5 (opens in a new tab)CAS3005889-81-3
Parent
Analog of GLP-1The GLP-1 agonist moiety joins a disulfide-free calcitonin-based amylin-receptor agonist moiety. It is not one contiguous native GLP-1 fragment.
Development
Phase 3Novo NordiskNCT05369390 and NCT06064006 completed with actual enrollments of 144 and 125. Publications confirm participant treatment. NCT07339423 is a recruiting phase 3 trial with estimated enrollment of 1150. Its estimate does not establish participant exposure. Source (opens in a new tab)

Targets

Molecular targets with action and evidence source
TargetActionEvidence
GLP1RGLP1RAgonistPrimary identity or pharmacology sourceSource (opens in a new tab)
CALCRCALCRAgonistPrimary 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

68 amino acids · 3 modifications

Residues 1 to 10:
HEGTFTSDV
Residues 11 to 20:
SSYLEEQAAR
Residues 21 to 30:
EFIAWLVRGR
Residues 31 to 40:
GGGGEASEL
Residues 41 to 50:
STAALGRLSA
Residues 51 to 60:
ELHELATLPR
Residues 61 to 68:
TETGSGSP
  • HydrophobicA V I L M
  • AromaticF W Y
  • PositiveK R H
  • NegativeD E
  • PolarS T N Q
  • SpecialC G P
  • Non-canonicalX
  • Modified residue

Modifications

Aib2
Non-canonical residue
Residue 2 is 2-aminoisobutyric acid (Aib), represented by X in the GSRS sequence. Aib is achiral.
GLP-1 position 37
Albumin-binding group
Lys31 N6 carries a C18 diacid-based albumin-binding side chain through two AEEA units and gamma-glutamate. WHO specifies the side-chain stereocentre as 22S.
68
C-terminal amide
C-terminal carboxamide.

Alignment to GLP-1

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

28 of 31 aligned residues identical (90%) · 2 substitutions · 1 non-canonical residue · 37 added residues · 1 modified residue · GLP-1 1–31

  • Top row: GLP-1 (parent)
  • Bottom row: Amycretin
HEGTFTSDV
SSYLEQAA
EFIAWLV
G
R
G
  • Same as parent
  • Substituted
  • Non-canonical or D-form
  • Added
  • Gap
  • Modified side chain or end

Differences from the parent

  1. 1Parent 2 · analog 2Ala → Aib · Non-canonical residueResidue 2 is 2-aminoisobutyric acid (Aib), represented by X in the GSRS sequence. Aib is achiral.
  2. 2Parent 16 · analog 16Gly → Glu · Substitution
  3. 3Parent 20 · analog 20Lys → Arg · Substitution
  4. 4Not in parent · analog 28+ Arg · Added residue
  5. 5Not in parent · analog 29+ Gly · Added residue
  6. 6Not in parent · analog 30+ Arg · Added residue
  7. 7Parent 28 · analog 31Lys, modified · Albumin-binding groupLys31 N6 carries a C18 diacid-based albumin-binding side chain through two AEEA units and gamma-glutamate. WHO specifies the side-chain stereocentre as 22S.
  8. 8Not in parent · analog 32+ Gly · Added residue
  9. 9Not in parent · analog 33+ Gly · Added residue
  10. 10Not in parent · analog 34+ Gly · Added residue
  11. 11Not in parent · analog 35+ Gly · Added residue
  12. 12Not in parent · analog 36+ Glu · Added residue
  13. 13Not in parent · analog 37+ Ala · Added residue
  14. 14Not in parent · analog 38+ Ser · Added residue
  15. 15Not in parent · analog 39+ Glu · Added residue
  16. 16Not in parent · analog 40+ Leu · Added residue
  17. 17Not in parent · analog 41+ Ser · Added residue
  18. 18Not in parent · analog 42+ Thr · Added residue
  19. 19Not in parent · analog 43+ Ala · Added residue
  20. 20Not in parent · analog 44+ Ala · Added residue
  21. 21Not in parent · analog 45+ Leu · Added residue
  22. 22Not in parent · analog 47+ Arg · Added residue
  23. 23Not in parent · analog 48+ Leu · Added residue
  24. 24Not in parent · analog 49+ Ser · Added residue
  25. 25Not in parent · analog 50+ Ala · Added residue
  26. 26Not in parent · analog 51+ Glu · Added residue
  27. 27Not in parent · analog 52+ Leu · Added residue
  28. 28Not in parent · analog 53+ His · Added residue
  29. 29Not in parent · analog 54+ Glu · Added residue
  30. 30Not in parent · analog 55+ Leu · Added residue
  31. 31Not in parent · analog 56+ Ala · Added residue
  32. 32Not in parent · analog 57+ Thr · Added residue
  33. 33Not in parent · analog 58+ Leu · Added residue
  34. 34Not in parent · analog 59+ Pro · Added residue
  35. 35Not in parent · analog 61+ Thr · Added residue
  36. 36Not in parent · analog 62+ Glu · Added residue
  37. 37Not in parent · analog 63+ Thr · Added residue
  38. 38Not in parent · analog 64+ Gly · Added residue
  39. 39Not in parent · analog 65+ Ser · Added residue
  40. 40Not in parent · analog 67+ Ser · Added residue
  41. 41Not in parent · analog 68+ Pro · Added residueC-terminal carboxamide.

Basis: The GLP-1 agonist moiety joins a disulfide-free calcitonin-based amylin-receptor agonist moiety. It is not one contiguous native GLP-1 fragment.

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
C343H550N94O116
Molecular weight
7,846.686 g/mol

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)
6,990 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: albumin-binding group. 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

  • Hydrophobic28% (19)
  • Aromatic6% (4)
  • Positive12% (8)
  • Negative15% (10)
  • Polar22% (15)
  • Special16% (11)
  • Non-canonical1% (1)

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

A Ala8 · 12%
I Ile1 · 1%
L Leu8 · 12%
M Met0 · 0%
V Val2 · 3%
F Phe2 · 3%
W Trp1 · 1%
Y Tyr1 · 1%
H His2 · 3%
K Lys1 · 1%
R Arg5 · 7%
D Asp1 · 1%
E Glu9 · 13%
N Asn0 · 0%
Q Gln1 · 1%
S Ser8 · 12%
T Thr6 · 9%
C Cys0 · 0%
G Gly9 · 13%
P Pro2 · 3%
X Xaa1 · 1%

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.

Helical wheel of Amycretin, 54 residues at 100 degrees per residue. Hydrophobic moment 0.08 pointing at 333 degrees.His 1, Eisenberg consensus (normalized) -0.40H1Non-canonical 2X2Glu 3, Eisenberg consensus (normalized) -0.74E−3Gly 4, Eisenberg consensus (normalized) 0.48G4Thr 5, Eisenberg consensus (normalized) -0.05T5Phe 6, Eisenberg consensus (normalized) 1.19F6Thr 7, Eisenberg consensus (normalized) -0.05T7Ser 8, Eisenberg consensus (normalized) -0.18S8Asp 9, Eisenberg consensus (normalized) -0.90D−9Val 10, Eisenberg consensus (normalized) 1.08V10Ser 11, Eisenberg consensus (normalized) -0.18S11Ser 12, Eisenberg consensus (normalized) -0.18S12Tyr 13, Eisenberg consensus (normalized) 0.26Y13Leu 14, Eisenberg consensus (normalized) 1.06L14Glu 15, Eisenberg consensus (normalized) -0.74E−15Glu 16, Eisenberg consensus (normalized) -0.74E−16Gln 17, Eisenberg consensus (normalized) -0.85Q17Ala 18, Eisenberg consensus (normalized) 0.62A18Ala 19, Eisenberg consensus (normalized) 0.62A19Arg 20, Eisenberg consensus (normalized) -2.53R+20Glu 21, Eisenberg consensus (normalized) -0.74E−21Phe 22, Eisenberg consensus (normalized) 1.19F22Ile 23, Eisenberg consensus (normalized) 1.38I23Ala 24, Eisenberg consensus (normalized) 0.62A24Trp 25, Eisenberg consensus (normalized) 0.81W25Leu 26, Eisenberg consensus (normalized) 1.06L26Val 27, Eisenberg consensus (normalized) 1.08V27Arg 28, Eisenberg consensus (normalized) -2.53R+28Gly 29, Eisenberg consensus (normalized) 0.48G29Arg 30, Eisenberg consensus (normalized) -2.53R+30Lys 31, Eisenberg consensus (normalized) -1.50K+31Gly 32, Eisenberg consensus (normalized) 0.48G32Gly 33, Eisenberg consensus (normalized) 0.48G33Gly 34, Eisenberg consensus (normalized) 0.48G34Gly 35, Eisenberg consensus (normalized) 0.48G35Glu 36, Eisenberg consensus (normalized) -0.74E−36Ala 37, Eisenberg consensus (normalized) 0.62A37Ser 38, Eisenberg consensus (normalized) -0.18S38Glu 39, Eisenberg consensus (normalized) -0.74E−39Leu 40, Eisenberg consensus (normalized) 1.06L40Ser 41, Eisenberg consensus (normalized) -0.18S41Thr 42, Eisenberg consensus (normalized) -0.05T42Ala 43, Eisenberg consensus (normalized) 0.62A43Ala 44, Eisenberg consensus (normalized) 0.62A44Leu 45, Eisenberg consensus (normalized) 1.06L45Gly 46, Eisenberg consensus (normalized) 0.48G46Arg 47, Eisenberg consensus (normalized) -2.53R+47Leu 48, Eisenberg consensus (normalized) 1.06L48Ser 49, Eisenberg consensus (normalized) -0.18S49Ala 50, Eisenberg consensus (normalized) 0.62A50Glu 51, Eisenberg consensus (normalized) -0.74E−51Leu 52, Eisenberg consensus (normalized) 1.06L52His 53, Eisenberg consensus (normalized) -0.40H53Glu 54, Eisenberg consensus (normalized) -0.74E−54
μH, residues shown
0.081
μH, best 11-residue window
—
Arrow direction
333°
Residues
1–54 of 68 · 3 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
PositionResidueAngleEisenberg consensus (normalized)
1H0°-0.40
2X100°not scored
3E200°-0.74
4G300°0.48
5T40°-0.05
6F140°1.19
7T240°-0.05
8S340°-0.18
9D80°-0.90
10V180°1.08
11S280°-0.18
12S20°-0.18
13Y120°0.26
14L220°1.06
15E320°-0.74
16E60°-0.74
17Q160°-0.85
18A260°0.62
19A0°0.62
20R100°-2.53
21E200°-0.74
22F300°1.19
23I40°1.38
24A140°0.62
25W240°0.81
26L340°1.06
27V80°1.08
28R180°-2.53
29G280°0.48
30R20°-2.53
31K120°-1.50
32G220°0.48
33G320°0.48
34G60°0.48
35G160°0.48
36E260°-0.74
37A0°0.62
38S100°-0.18
39E200°-0.74
40L300°1.06
41S40°-0.18
42T140°-0.05
43A240°0.62
44A340°0.62
45L80°1.06
46G180°0.48
47R280°-2.53
48L20°1.06
49S120°-0.18
50A220°0.62
51E320°-0.74
52L60°1.06
53H160°-0.40
54E260°-0.74
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