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Peptide·plain sequence-like

ATLPC0000870

ATLPC0000870

IKPEAPGEDASPEELNRYYASLRHYLNLVTRQRY

Routes
Compare in workbenchDownload releaseAPI JSON
  • Length
    34 aa
  • Monoisotopic mass
    4048.1 Da
  • Net charge @ pH 7.4
    0.10
  • Isoelectric point
    7.52
  • GRAVY
    -1.074
On this page
  • 01 Sequence & molecular identity
  • 02 Physicochemical profile
  • 03 Distribution / Barrier
  • 04 Metabolic & Proteolytic Stability
  • 05 Excretion / Persistence
  • 06 Evidence landscape
  • 07 Product context
  • 08 Identity & reference map
  • 09 Data access & reproducibility
Coveragecounts only · not riskATLPC0000870
  • Measurements
    50
  • Endpoints
    3
  • Domains
    3/5
  • Products
    —
  • 4 stability measurements
  • 24 clearance measurements
  • No immunogenicity context
  • No sequence liability cues
Jump to domain

Open the matching evidence section below

All evidence index · 50
Exposure / Absorption
No evidence
Distribution / Barrier
22 measurements
Metabolic & Proteolytic Stability
4 measurements
Excretion / Persistence
24 measurements
Toxicity / Safety
No evidence
01

Sequence & molecular identity

1 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
34
Peptidoform features
0
Documented molecular forms
1
Representations
2
Documented molecular forms1 form linked to this peptide identity
FormTopologyModificationsConnectionsRepresentationsMeasurements
ATLPF0000961———Notation only2
Residue view
Residue display
34 residues
I1K2P3E4A5P6G7E8D9A10S11P12E13E14L15N16R17Y18Y19A20S21L22R23H24Y25L26N27L28V29T30R31Q32R33Y34
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.

IKPEAPGEDASPEELNRYYASLRHYLNLVTRQRY
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 references1 reference
3D coordinates·Exact PDB matchexperimental
Exact PDB match·reference selected·length 34 aa·confidence experimental
LinkMethodConfidenceMatch
OpenExperimental coordinate entryexperimental34 aa
Covalent topology & modificationsnone
Exact topology not established

No reviewed form-level topology or residue-level connection annotation is attached to this peptide in the current release. This is not evidence that every molecular form is linear or unmodified.

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 descriptors34 aa · pI 7.5 · GRAVY -1.07
Length
34 aa
Monoisotopic mass
4048.06 Da
Average mass
4050.50 Da
Net charge at pH 7.4
0.10
Estimated pI
7.52
GRAVY
-1.074
KD-positive residues
26.5%
Aromatic residues
11.8%
Developability interpretation
Ionization context
pH 7.4 close to pI
Hydrophobicity balance
Leans hydrophilic
Amphipathic moment (μH)
0.74
Computation boundary
Standard-sequence only
Charge & residue composition
pH charge context

Modeled net charge across common formulation and assay pH checkpoints.

pH 2
6.93
pH 5
1.53
pH 6
0.82
pH 7.4
0.05
pH 9
-1.02
pH 12
-6.85
Residue-class composition

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

Acidic (D,E)
5 · 14.7%
Basic (K,R,H)
6 · 17.6%
Polar uncharged (N,Q,S,T)
6 · 17.6%
Hydrophobic aliphatic (A,V,I,L,M)
9 · 26.5%
Aromatic (F,W,Y)
4 · 11.8%
Conformational / sulfur (G,P,C)
4 · 11.8%
Top residues
R411.8%E411.8%L411.8%Y411.8%A38.8%P38.8%N25.9%S25.9%
Hydropathy & amphipathic windows
Hydropathy windows

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

Most hydrophobic window
24-30
HYLNLVT
GRAVY 0.443
Most hydrophilic window
8-14
EDASPEE
GRAVY -2.086
28 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
21-32
SLRHYLNLVTRQ
μH 1.56 · charge 2.1
12 aa window
20-31
ASLRHYLNLVTR
μH 1.53 · charge 2.1
15 aa window
13-27
EELNRYYASLRHYLN
μH 1.42 · charge 0.1
15 aa window
15-29
LNRYYASLRHYLNLV
μH 1.38 · charge 2.1
12 aa window
13-24
EELNRYYASLRH
μH 1.35 · charge 0.1
Sequence-liability cues
Sequence-liability notes

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

No conservative sequence-liability motifs from the current rule set are present.
Alpha-helix amphipathic projection
Helical wheel · Edmundson projection
μH = 0.74100°/residue · 34 aa
μH1: I (Ile) · Hydrophobic · K-D 4.5I12: K (Lys) · Basic + · K-D -3.9K3: P (Pro) · Special · K-D -1.6P4: E (Glu) · Acidic − · K-D -3.5E5: A (Ala) · Hydrophobic · K-D 1.8A56: P (Pro) · Special · K-D -1.6P7: G (Gly) · Special · K-D -0.4G8: E (Glu) · Acidic − · K-D -3.5E9: D (Asp) · Acidic − · K-D -3.5D10: A (Ala) · Hydrophobic · K-D 1.8A1011: S (Ser) · Polar · K-D -0.8S12: P (Pro) · Special · K-D -1.6P13: E (Glu) · Acidic − · K-D -3.5E14: E (Glu) · Acidic − · K-D -3.5E15: L (Leu) · Hydrophobic · K-D 3.8L1516: N (Asn) · Polar · K-D -3.5N17: R (Arg) · Basic + · K-D -4.5R18: Y (Tyr) · Aromatic · K-D -1.3Y19: Y (Tyr) · Aromatic · K-D -1.3Y20: A (Ala) · Hydrophobic · K-D 1.8A2021: S (Ser) · Polar · K-D -0.8S22: L (Leu) · Hydrophobic · K-D 3.8L23: R (Arg) · Basic + · K-D -4.5R24: H (His) · Basic + · K-D -3.2H25: Y (Tyr) · Aromatic · K-D -1.3Y2526: L (Leu) · Hydrophobic · K-D 3.8L27: N (Asn) · Polar · K-D -3.5N28: L (Leu) · Hydrophobic · K-D 3.8L29: V (Val) · Hydrophobic · K-D 4.2V30: T (Thr) · Polar · K-D -0.7T3031: R (Arg) · Basic + · K-D -4.5R32: Q (Gln) · Polar · K-D -3.5Q33: R (Arg) · Basic + · K-D -4.5R34: Y (Tyr) · Aromatic · K-D -1.3Y34
Hydrophobic moment0.74
Mean K-D hydropathy-1.07
Approx. net charge0
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
74.71
Instability index
80.4

Above 40 — predicted unstable in vitro.

Boman index
2.93 kcal/mol

Above 2.48 — elevated potential protein-binding.

Molar extinction coefficient (280 nm)
5,960 M⁻¹·cm⁻¹

A280 (1 g/L) ≈ 1.47

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

Distribution / Barrier

22 records

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

Evidence records
22
Complete canonical measurements and observations attached to this domain.
Endpoint scope
1
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 penetration
Loading 22 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

04

Metabolic & Proteolytic Stability

4 records

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

Evidence records
4
Complete canonical measurements and observations attached to this domain.
Endpoint scope
1
Formal ADMET endpoints represented for this peptide.
Matched-context in preview
3
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 scopeSerum/plasma stability
Loading 4 Metabolic & Proteolytic Stability records…
05

Excretion / Persistence

24 records

What evidence describes clearance or persistence?

Evidence records
24
Complete canonical measurements and observations attached to this domain.
Endpoint scope
1
Formal ADMET endpoints represented for this peptide.
Matched-context in preview
17
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 scopeHalf Life
Loading 24 Excretion / Persistence records…
06

Evidence landscape

50 records

Cross-domain evidence distribution and measurement-level detail. 20 of 50 evidence records are included in the profile preview; the full index is loaded below.

Loading 50 measurements…
07

Product context

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

No product association in this release

This peptide is currently interpreted from sequence, structure, physicochemical, and ADMET evidence only.

Browse products
08

Identity & reference map

50 sources

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

·
Summary4 reference groups
Identity type
canonical sequence
Reported notation
0
Reference groups
4
Measurements
50
ATL peptide ID
ATLPC0000870
Identity concordance
Identity concordance
Exact reported notation

Reported sequence string matches the current peptide notation.

0 / 50
Parent-residue compatible

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

0 / 50
Different notation

Reported notation does not resolve to the current display sequence.

0 / 50
Source sequence not captured

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

50 / 50
Reported sequence notation

No source-specific sequence notation has been captured in the current identity references.

Current identity
IKPEAPGEDASPEELNRYYASLRHYLNLVTRQRY
Reported names
No distinct human-readable aliases are exposed.
Reference map4 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
24 identity
17 evidence
Reference
Open
Identity only
No reported alias
22 identity
0 evidence
Reference
Open
Stability
Serum Plasma Stability
No reported alias
2 identity
2 evidence
Reference
Open
Stability
Serum Plasma Stability
No reported alias
2 identity
1 evidence
09

Data access & reproducibility

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

·
Record scopePublic release
ATL peptide ID
ATLPC0000870
Identity type
canonical sequence
ADMET endpoints
3
Evidence records
50
Reference groups
4
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/ATLPC0000870
open
curl -sS 'https://admetatlas.scbdd.com/api/v1/peptides/ATLPC0000870' \
  -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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