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Peptide·plain sequence-like

Exenatide

ATLPC0009237

HGEGTFTSDLSKQMEEEAVRLFIEWLKNGGPSSGAPPPS

Routes
Compare in workbenchDownload releaseAPI JSON
  • Length
    39 aa
  • Monoisotopic mass
    4185.0 Da
  • Net charge @ pH 7.4
    -2.90
  • Isoelectric point
    4.41
  • GRAVY
    -0.692
On this page
  • 01 Sequence & molecular identity
  • 02 Physicochemical profile
  • 03 Exposure / Absorption
  • 04 Distribution / Barrier
  • 05 Metabolic & Proteolytic Stability
  • 06 Excretion / Persistence
  • 07 Evidence landscape
  • 08 Product context
  • 09 Identity & reference map
  • 10 Data access & reproducibility
Coveragecounts only · not riskATLPC0009237
  • Measurements
    143
  • Endpoints
    11
  • Domains
    4/5
  • Products
    1
  • 14 stability measurements
  • 86 clearance measurements
  • 6 immunogenicity context entries
  • 2 liability motifs
Jump to domain

Open the matching evidence section below

All evidence index · 143
Exposure / Absorption
14 measurements
Distribution / Barrier
29 measurements
Metabolic & Proteolytic Stability
14 measurements
Excretion / Persistence
86 measurements
Toxicity / Safety
No evidence
01

Sequence & molecular identity

2 forms

Reviewed sequence, peptidoform forms, chemical representation, 3D references, and covalent topology used to interpret this peptide identity.

Sequence & peptidoform

·
Identity summaryCanonical sequence only
Identity status
Canonical sequence only
Residues
39
Peptidoform features
0
Documented molecular forms
2
Representations
2
Documented molecular forms2 forms linked to this peptide identity
FormTopologyModificationsConnectionsRepresentationsMeasurements
ATLPF0010088—1—Notation only14
ATLPF0039585—1—Notation only6
Residue view
Residue display
39 residues
H1G2E3G4T5F6T7S8D9L10S11K12Q13M14E15E16E17A18V19R20L21F22I23E24W25L26K27N28G29G30P31S32S33G34A35P36P37P38S39
Secondary structureα-helix (H)β-strand (E)coil (C)
Side-chain classNonpolarPolarBasic (+)Acidic (−)Modified

Soft tints mark standard side-chain classes for scanning. Primary emphasis is reserved for reported modifications, termini, secondary-structure tracks, and topology links.

Peptidoform features

Features are shown only when a reported notation or topology record supports them.

No terminal modification, residue-level marker, disulfide, staple, coordination, or other topology signal is currently available.

Structure & chemistry

·
Chemical representationsequence / HELM only
Representation class

How the current release can interpret this identity chemically.

plain sequence-like
Parent-residue sequence

Residue string used for positional interpretation when available.

HGEGTFTSDLSKQMEEEAVRLFIEWLKNGGPSSGAPPPS
HELM

Polymer notation for modified peptide representation when available.

Not available
SMILES

Chemical graph string used for atom-level 2D depiction when available.

Not available
No atom-level graph

A reviewed SMILES is required before a 2D molecular depiction can be shown. Sequence and HELM remain useful for identity interpretation, but they do not replace a chemical graph.

3D structure references11 references
Structure reference·
3D coordinates·Sequence matchexperimental
Sequence match·reference selected·identity 100.0%·confidence experimental
LinkMethodConfidenceMatch
OpenSequence matchexperimental100.0% identity
OpenSequence matchexperimental100.0% identity
OpenSequence matchexperimental100.0% identity
OpenSequence matchexperimental100.0% identity
OpenSequence matchexperimental100.0% identity
OpenSequence matchexperimental100.0% identity
OpenSequence matchexperimental97.4% identity
OpenSequence matchexperimental97.4% identity
OpenSequence matchexperimental96.7% identity
OpenExperimental coordinate entryexperimental39 aa
OpenExperimental coordinate entryexperimental39 aa
Covalent topology & modifications1 signal
FeaturePositionsInterpretationLink
Form-level topologyATLPF0039585Open-chain form. Residue-level connection endpoints are shown separately when available.Not linked
02

Physicochemical profile

4 descriptors

Computed sequence-derived descriptors and any measured physicochemical evidence such as lipophilicity. Computed values are interpretation aids, not experimental ADMET measurements.

·
Core descriptors39 aa · pI 4.4 · GRAVY -0.69
Length
39 aa
Monoisotopic mass
4185.01 Da
Average mass
4187.61 Da
Net charge at pH 7.4
-2.90
Estimated pI
4.41
GRAVY
-0.692
KD-positive residues
25.6%
Aromatic residues
7.7%
Developability interpretation
Ionization context
pH 7.4 separated from pI
Hydrophobicity balance
Leans hydrophilic
Amphipathic moment (μH)
0.52
Computation boundary
Standard-sequence only
Charge & residue composition
pH charge context

Modeled net charge across common formulation and assay pH checkpoints.

pH 2
4.92
pH 5
-1.36
pH 6
-2.17
pH 7.4
-2.95
pH 9
-3.74
pH 12
-6.12
Residue-class composition

Grouped composition is often more interpretable than a long amino-acid list.

Acidic (D,E)
6 · 15.4%
Basic (K,R,H)
4 · 10.3%
Polar uncharged (N,Q,S,T)
9 · 23.1%
Hydrophobic aliphatic (A,V,I,L,M)
8 · 20.5%
Aromatic (F,W,Y)
3 · 7.7%
Conformational / sulfur (G,P,C)
9 · 23.1%
Top residues
E512.8%G512.8%S512.8%P410.3%L37.7%A25.1%K25.1%F25.1%
Hydropathy & amphipathic windows
Hydropathy windows

Seven-residue sliding windows expose local patches hidden by whole-sequence GRAVY.

Most hydrophobic window
17-23
EAVRLFI
GRAVY 1.300
Most hydrophilic window
11-17
SKQMEEE
GRAVY -2.400
33 local hydropathy windows scanned. A local patch is context for solubility, adsorption, and membrane interaction review, not a standalone endpoint.
Amphipathic-window scan

Top alpha-helix hydrophobic-moment windows across 12, 15, 18, and 21 residues.

12 aa window
17-28
EAVRLFIEWLKN
μH 1.99 · charge 0.0
12 aa window
16-27
EEAVRLFIEWLK
μH 1.87 · charge -1.0
12 aa window
18-29
AVRLFIEWLKNG
μH 1.69 · charge 1.0
15 aa window
17-31
EAVRLFIEWLKNGGP
μH 1.66 · charge 0.0
15 aa window
16-30
EEAVRLFIEWLKNGG
μH 1.61 · charge -1.0
Sequence-liability cues
Sequence-liability notes

Motifs are review prompts for formulation or CMC interpretation; they are not degradation predictions.

Asn deamidation motif
NG · pos 28
Asn followed by small/polar residues is a known sequence context to review for deamidation susceptibility.
Oxidation-sensitive residues
M, W · pos 14, 25
Met, Trp, and Cys residues can merit formulation review for oxidation or covalent-state sensitivity.
Alpha-helix amphipathic projection
Helical wheel · Edmundson projection
μH = 0.52100°/residue · 39 aa
μH1: H (His) · Basic + · K-D -3.2H12: G (Gly) · Special · K-D -0.4G3: E (Glu) · Acidic − · K-D -3.5E4: G (Gly) · Special · K-D -0.4G5: T (Thr) · Polar · K-D -0.7T56: F (Phe) · Aromatic · K-D 2.8F7: T (Thr) · Polar · K-D -0.7T8: S (Ser) · Polar · K-D -0.8S9: D (Asp) · Acidic − · K-D -3.5D10: L (Leu) · Hydrophobic · K-D 3.8L1011: S (Ser) · Polar · K-D -0.8S12: K (Lys) · Basic + · K-D -3.9K13: Q (Gln) · Polar · K-D -3.5Q14: M (Met) · Hydrophobic · K-D 1.9M15: E (Glu) · Acidic − · K-D -3.5E1516: E (Glu) · Acidic − · K-D -3.5E17: E (Glu) · Acidic − · K-D -3.5E18: A (Ala) · Hydrophobic · K-D 1.8A19: V (Val) · Hydrophobic · K-D 4.2V20: R (Arg) · Basic + · K-D -4.5R2021: L (Leu) · Hydrophobic · K-D 3.8L22: F (Phe) · Aromatic · K-D 2.8F23: I (Ile) · Hydrophobic · K-D 4.5I24: E (Glu) · Acidic − · K-D -3.5E25: W (Trp) · Aromatic · K-D -0.9W2526: L (Leu) · Hydrophobic · K-D 3.8L27: K (Lys) · Basic + · K-D -3.9K28: N (Asn) · Polar · K-D -3.5N29: G (Gly) · Special · K-D -0.4G30: G (Gly) · Special · K-D -0.4G3031: P (Pro) · Special · K-D -1.6P32: S (Ser) · Polar · K-D -0.8S33: S (Ser) · Polar · K-D -0.8S34: G (Gly) · Special · K-D -0.4G35: A (Ala) · Hydrophobic · K-D 1.8A3536: P (Pro) · Special · K-D -1.6P37: P (Pro) · Special · K-D -1.6P38: P (Pro) · Special · K-D -1.6P39: S (Ser) · Polar · K-D -0.8S39
Hydrophobic moment0.52
Mean K-D hydropathy-0.69
Approx. net charge-3
Projection angle100° / residue
The pale sector marks the direction of the hydrophobic face inferred from μH. This is a projection assumption, not a measured fold.
HydrophobicAromaticPolarBasic +Acidic −Specialhydrophobic faceμH arrow → hydrophobic face

The projection assumes an α-helix conformation; a long μH arrow indicates an amphipathic helix, common in antimicrobial peptides.Sequence > 30 aa — only termini and every fifth position are numbered because later turns share earlier wheel angles.

Method notes

Charge model: side-chain pKa D 3.9, E 4.1, C 8.5, Y 10.1, H 6.5, K 10.8, R 12.5 with EMBOSS termini. pI is estimated by binary search on modeled net charge. Hydropathy uses Kyte-Doolittle values; hydrophobic moment follows the Eisenberg alpha-helix vector-sum convention. When the basis is a parent-residue sequence, modified chemistry is intentionally not inferred.

Computed developability descriptors

Deterministic descriptors computed from the reviewed sequence or chemical structure (RDKit), each anchored to a literature method. These are computed estimates for developability interpretation — not experimental measurements — and are validated against independent reference implementations.

Sequence-derived

Computed from the standard parent-residue sequence; protein-origin metrics defined at any length.

Aliphatic index
52.56
Instability index
64.1

Above 40 — predicted unstable in vitro.

Boman index
1.67 kcal/mol
Molar extinction coefficient (280 nm)
5,500 M⁻¹·cm⁻¹

A280 (1 g/L) ≈ 1.31

Structure-derived descriptors are not shown because this identity has no resolved chemical structure (SMILES). This is a known coverage gap for disulfide-rich and unresolved peptidoforms, not a computation error.

03

Exposure / Absorption

14 records

What evidence describes systemic exposure or absorption?

Evidence records
14
Complete canonical measurements and observations attached to this domain.
Endpoint scope
4
Formal ADMET endpoints represented for this peptide.
Matched-context in preview
0
Quantitative results that may be analysed only with scientifically compatible records.
Reported results in preview
0
Qualitative, narrative, or review-first results interpreted in their source context.
Endpoints in scopeAUCBioavailabilityCmaxTmax
Loading 14 Exposure / Absorption records…
04

Distribution / Barrier

29 records

What is known about distribution, binding, permeability, or barrier crossing?

Evidence records
29
Complete canonical measurements and observations attached to this domain.
Endpoint scope
3
Formal ADMET endpoints represented for this peptide.
Matched-context in preview
0
Quantitative results that may be analysed only with scientifically compatible records.
Reported results in preview
0
Qualitative, narrative, or review-first results interpreted in their source context.
Endpoints in scopeBBB penetrationPlasma protein bindingVd
Loading 29 Distribution / Barrier records…
Barrier and permeability assay context

PAMPA, Caco-2, MDCK/RRCK, and BBB findings are assay/model contexts under Distribution / Barrier. They should not be read as interchangeable measurements.

PAMPA
0

artificial membrane

Caco-2
0

cell monolayer

MDCK
0

cell monolayer

RRCK
0

cell monolayer

BBB
0

barrier evidence

05

Metabolic & Proteolytic Stability

14 records

How stable is the peptide in biological matrices or protease systems?

Evidence records
14
Complete canonical measurements and observations attached to this domain.
Endpoint scope
2
Formal ADMET endpoints represented for this peptide.
Matched-context in preview
2
Quantitative results that may be analysed only with scientifically compatible records.
Reported results in preview
0
Qualitative, narrative, or review-first results interpreted in their source context.
Endpoints in scopeProtease stabilitySerum/plasma stability
Loading 14 Metabolic & Proteolytic Stability records…
06

Excretion / Persistence

86 records

What evidence describes clearance or persistence?

Evidence records
86
Complete canonical measurements and observations attached to this domain.
Endpoint scope
2
Formal ADMET endpoints represented for this peptide.
Matched-context in preview
5
Quantitative results that may be analysed only with scientifically compatible records.
Reported results in preview
9
Qualitative, narrative, or review-first results interpreted in their source context.
Endpoints in scopeHalf LifeClearance
Loading 86 Excretion / Persistence records…
07

Evidence landscape

143 records

Cross-domain evidence distribution and measurement-level detail. 20 of 143 evidence records are included in the profile preview; the full index is loaded below.

Loading 143 measurements…
08

Product context

1 products

Product-level route, label, and clinical context that frames peptide-level evidence. A peptide-level summary only; product pages keep the full drilldown.

·
Summary1 linked product
Linked products
1
Label context
1
Clinical trials
25
Safety label cues
8
Linked products1 shown

Exenatide

BYETTABYDUREON
Peptide-product match
Reviewed peptide match
Route / product class
parenteral_other · Hypoglycemic Agents
Clinical context
25 trial records · 14 exact intervention matches · 5 with results · latest 2026-02-24
Label safety context
Label linked · Contraindications · Adverse reactions · Clinical AE review · Immunogenicity review
View product
09

Identity & reference map

143 sources

Reference-level support for checking reported names, sequence notation, and peptide identity agreement.

·
Summary43 reference groups
Identity type
canonical sequence
Reported notation
2
Reference groups
43
Measurements
143
ATL peptide ID
ATLPC0009237
Identity concordance
Identity concordance
Exact reported notation

Reported sequence string matches the current peptide notation.

2 / 143
Parent-residue compatible

Reported notation differs, but resolves to the same parent-residue display.

0 / 143
Different notation

Reported notation does not resolve to the current display sequence.

2 / 143
Source sequence not captured

No source-specific sequence was captured for comparison; this is not interpreted as agreement or disagreement.

139 / 143
Reported sequence notation
Exact2 references
HGEGTFTSDLSKQMEEEAVRLFIEWLKNGGPSSGAPPPS
Different2 references
HGEGTFTSDLSKQMEEEAVRLFIEWLKNGGPSSGAPPPS-NH2
Current identity
HGEGTFTSDLSKQMEEEAVRLFIEWLKNGGPSSGAPPPS
Reported names
brainpeps_observation_v2_16_27_6_2a5911d1b8e0a2821269brainpeps_observation_v2_16_27_6_2cb58b7b10c7f504b0f6
Reference map43 reference groups
Reference map

Grouped by reference link, with endpoint scope and reported identity kept visible.

ReferenceSupportsReported identityRecords
Reference
Open
Persistence
Half Life
No reported alias
21 identity
6 evidence
Reference
Open
Identity only
brainpeps_observation_v2_16_27_6_2a5911d1b8e0a2821269, brainpeps_observation_v2_16_27_6_2cb58b7b10c7f504b0f6
HGEGTFTSDLSKQMEEEAVRLFIEWLKNGGPSSGAPPPSexact
23 identity
0 evidence
Reference
Open
Persistence
Half Life
No reported alias
13 identity
2 evidence
Reference
Open
Persistence
Half Life
No reported alias
9 identity
3 evidence
Reference
Open
Stability
Protease Stability
No reported alias
8 identity
2 evidence
Reference
Open
Persistence
Half Life
No reported alias
6 identity
2 evidence
Reference
Open
Identity only
No reported alias
8 identity
0 evidence
Reference
Open
Persistence
Half Life
No reported alias
4 identity
2 evidence
Reference
Open
Persistence
Half Life
No reported alias
3 identity
1 evidence
Reference
Open
Persistence
Half Life
No reported alias
2 identity
1 evidence
1–10 / 43
10

Data access & reproducibility

Stable record access, analysis-ready files, and scripted retrieval for reproducing this profile view.

·
Record scopePublic release
ATL peptide ID
ATLPC0009237
Identity type
canonical sequence
ADMET endpoints
11
Evidence records
143
Reference groups
43
Release view
Public release
Data access

Structured peptide profile

JSON

Peptide-specific profile used by this page, including identity and evidence context.

Open JSON

Peptide catalogue

TSV

Complete frozen peptide table. Filter the ATL peptide ID column locally to isolate this record.

Download catalogue

Measurement catalogue

TSV

Complete frozen measurement table. Join or filter by ATL peptide ID for peptide-level analysis.

Download measurements
Programmatic access

The request returns the same structured peptide record used by this profile. The tabular downloads are complete frozen release tables and should be filtered locally by ATL peptide ID.

Open endpoint
GET /api/v1/peptides/ATLPC0009237
open
curl -sS 'https://admetatlas.scbdd.com/api/v1/peptides/ATLPC0009237' \
  -H 'accept: application/json' \
  -H 'X-Visibility: public_release'
ADMETatlas
peptide evidence atlas

ADMETatlas is an open, curated atlas of ADMET evidence for therapeutic peptides — spanning developability, membrane permeability and blood–brain-barrier transport, immune-recognition context, and approved-product context. Every measurement stays linked to its original source, with stable identifiers and transparent curation, so results can be traced, cited, and reproduced.

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© 2026 ADMETatlas, an academic peptide ADMET evidence atlas.