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  3. Indolicidin (1-12)
Peptide·plain sequence-like

Indolicidin (1-12)

ATLPC0012858

ILPWKWPWWPWR

Compare in workbenchDownload releaseAPI JSON
  • Length
    12 aa
  • Monoisotopic mass
    1749.9 Da
  • Net charge @ pH 7.4
    2.00
  • Isoelectric point
    11.65
  • GRAVY
    -0.783
On this page
  • 01 Sequence & molecular identity
  • 02 Physicochemical profile
  • 03 Evidence landscape
  • 04 Product context
  • 05 Identity & reference map
  • 06 Data access & reproducibility
Coveragecounts only · not riskATLPC0012858
  • Measurements
    0
  • Endpoints
    0
  • Domains
    0/5
  • Products
    —
  • No matrix stability evidence
  • No clearance evidence
  • No immunogenicity context
  • 2 liability motifs
Jump to domain

Open the matching evidence section below

All evidence index
Exposure / Absorption
No evidence
Distribution / Barrier
No evidence
Metabolic & Proteolytic Stability
No evidence
Excretion / Persistence
No evidence
Toxicity / Safety
No evidence
01

Sequence & molecular identity

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
12
Peptidoform features
0
Documented molecular forms
0
Representations
2
Documented molecular formsNo specific molecular form linked
Specific molecular form not established

The peptide identity is retained at sequence or backbone level, but the current evidence does not identify a specific chemical form. This is not evidence that the peptide is unmodified.

Residue view
Residue display
12 residues
I1L2P3W4K5W6P7W8W9P10W11R12
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.

ILPWKWPWWPWR
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 referencesnone attached
3D structure not available

A 3D structure isn't available for this peptide in the current release. Chemistry and topology fields remain available when represented by sequence, HELM, or SMILES.

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 descriptors12 aa · pI 11.7 · GRAVY -0.78
Length
12 aa
Monoisotopic mass
1749.93 Da
Average mass
1751.11 Da
Net charge at pH 7.4
2.00
Estimated pI
11.65
GRAVY
-0.783
KD-positive residues
16.7%
Aromatic residues
41.7%
Developability interpretation
Ionization context
pH 7.4 separated from pI
Hydrophobicity balance
Leans hydrophilic
Amphipathic moment (μH)
0.18
Computation boundary
Standard-sequence only
Charge & residue composition
pH charge context

Modeled net charge across common formulation and assay pH checkpoints.

pH 2
2.98
pH 5
2.04
pH 6
2.00
pH 7.4
1.94
pH 9
1.27
pH 12
-0.18
Residue-class composition

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

Basic (K,R,H)
2 · 16.7%
Hydrophobic aliphatic (A,V,I,L,M)
2 · 16.7%
Aromatic (F,W,Y)
5 · 41.7%
Conformational / sulfur (G,P,C)
3 · 25.0%
Top residues
W541.7%P325.0%R18.3%I18.3%L18.3%K18.3%
Hydropathy & amphipathic windows
Hydropathy windows

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

Most hydrophobic window
1-7
ILPWKWP
GRAVY -0.086
Most hydrophilic window
6-12
WPWWPWR
GRAVY -1.614
6 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
1-12
ILPWKWPWWPWR
μH 0.18 · charge 2.0
Sequence-liability cues
Sequence-liability notes

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

Oxidation-sensitive residues
W · pos 4, 6, 8, 9, 11
Met, Trp, and Cys residues can merit formulation review for oxidation or covalent-state sensitivity.
Pro/Gly-rich sequence
P/G · pos 3, 7, 10
High Pro/Gly content can affect local flexibility and secondary-structure propensity.
Alpha-helix amphipathic projection
Helical wheel · Edmundson projection
μH = 0.18100°/residue · 12 aa
μH1: I (Ile) · Hydrophobic · K-D 4.5I12: L (Leu) · Hydrophobic · K-D 3.8L23: P (Pro) · Special · K-D -1.6P34: W (Trp) · Aromatic · K-D -0.9W45: K (Lys) · Basic + · K-D -3.9K56: W (Trp) · Aromatic · K-D -0.9W67: P (Pro) · Special · K-D -1.6P78: W (Trp) · Aromatic · K-D -0.9W89: W (Trp) · Aromatic · K-D -0.9W910: P (Pro) · Special · K-D -1.6P1011: W (Trp) · Aromatic · K-D -0.9W1112: R (Arg) · Basic + · K-D -4.5R12
Hydrophobic moment0.18
Mean K-D hydropathy-0.78
Approx. net charge+2
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.

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
65.00
Instability index
34.1

At or below 40 — predicted stable in vitro.

Boman index
-0.09 kcal/mol
Molar extinction coefficient (280 nm)
27,500 M⁻¹·cm⁻¹

A280 (1 g/L) ≈ 15.70

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

Evidence landscape

Cross-domain evidence distribution and measurement-level detail. No assay-level evidence is available for this peptide in the current release.

No endpoint-level measurements returned

No ADMET endpoint evidence is attached to this peptide yet.

/evidence/drilldown
04

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
05

Identity & reference map

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

No identity references available

No reported identity references are available for this peptide in the current release.

06

Data access & reproducibility

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

·
Record scopePublic release
ATL peptide ID
ATLPC0012858
Identity type
canonical sequence
ADMET endpoints
0
Evidence records
0
Reference groups
1
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/ATLPC0012858
open
curl -sS 'https://admetatlas.scbdd.com/api/v1/peptides/ATLPC0012858' \
  -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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