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Peptide·map backed

ATLPC0026628

ATLPC0026628

MFTLKKSLFLVLILGMVSLSLCQQESNADKETTKEVTGEANTAGNVEIVEVAEVEKEMEELYKEIDDCVNYGNCKTLKLM

Compare in workbenchDownload releaseAPI JSON
  • Length
    80 aa
  • Monoisotopic mass
    8945.4 Da
  • Net charge @ pH 7.4
    -7.00
  • Isoelectric point
    4.14
  • GRAVY
    -0.085
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 riskATLPC0026628
  • Measurements
    0
  • Endpoints
    0
  • Domains
    0/5
  • Products
    —
  • No matrix stability evidence
  • No clearance evidence
  • No immunogenicity context
  • 3 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

1 forms

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

Sequence & peptidoform

·
Identity summarySpecific molecular form represented
Identity status
Specific molecular form represented
Residues
80
Peptidoform features
0
Documented molecular forms
1
Representations
4
Documented molecular forms1 form linked to this peptide identity
FormTopologyModificationsConnectionsRepresentationsMeasurements
ATLPF0028958———Notation only—
Residue view
Residue display
80 residues
M1F2T3L4K5K6S7L8F9L10V11L12I13L14G15M16V17S18L19S20L21C22Q23Q24E25S26N27A28D29K30E31T32T33K34E35V36T37G38E39A40N41T42A43G44N45V46E47I48V49E50V51A52E53V54E55K56E57M58E59E60L61Y62K63E64I65D66D67C68V69N70Y71G72N73C74K75T76L77K78L79M80
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 representationSMILES available
2D structure·RDKit.js
rendering molecule…
Canonical SMILES
CC[C@H](C)[C@H](NC(=O)[C@H](CC(C)C)NC(=O)[C@@H](NC(=O)[C@H](CC(C)C)NC(=O)[C@H](Cc1ccccc1)NC(=O)[C@H](CC(C)C)NC(=O)[C@H](CO)NC(=O)[C@H](CCCCN)NC(=O)[C@H](CCCCN)NC(=O)[C@H](CC(C)C)NC(=O)[C@@H](NC(=O)[C@H](Cc1ccccc1)NC(=O)[C@@H](N)CCSC)[C@@H](C)O)C(C)C)C(=O)N[C@@H](CC(C)C)C(=O)NCC(=O)N[C@@H](CCSC)C(=O)N[C@H](C(=O)N[C@@H](CO)C(=O)N[C@@H](CC(C)C)C(=O)N[C@@H](CO)C(=O)N[C@@H](CC(C)C)C(=O)N[C@@H](CS)C(=O)N[C@@H](CCC(N)=O)C(=O)N[C@@H](CCC(N)=O)C(=O)N[C@@H](CCC(=O)O)C(=O)N[C@@H](CO)C(=O)N[C@@H](CC(N)=O)C(=O)N[C@@H](C)C(=O)N[C@@H](CC(=O)O)C(=O)N[C@@H](CCCCN)C(=O)N[C@@H](CCC(=O)O)C(=O)N[C@H](C(=O)N[C@H](C(=O)N[C@@H](CCCCN)C(=O)N[C@@H](CCC(=O)O)C(=O)N[C@H](C(=O)N[C@H](C(=O)NCC(=O)N[C@@H](CCC(=O)O)C(=O)N[C@@H](C)C(=O)N[C@@H](CC(N)=O)C(=O)N[C@H](C(=O)N[C@@H](C)C(=O)NCC(=O)N[C@@H](CC(N)=O)C(=O)N[C@H](C(=O)N[C@@H](CCC(=O)O)C(=O)N[C@H](C(=O)N[C@H](C(=O)N[C@@H](CCC(=O)O)C(=O)N[C@H](C(=O)N[C@@H](C)C(=O)N[C@@H](CCC(=O)O)C(=O)N[C@H](C(=O)N[C@@H](CCC(=O)O)C(=O)N[C@@H](CCCCN)C(=O)N[C@@H](CCC(=O)O)C(=O)N[C@@H](CCSC)C(=O)N[C@@H](CCC(=O)O)C(=O)N[C@@H](CCC(=O)O)C(=O)N[C@@H](CC(C)C)C(=O)N[C@@H](Cc1ccc(O)cc1)C(=O)N[C@@H](CCCCN)C(=O)N[C@@H](CCC(=O)O)C(=O)N[C@H](C(=O)N[C@@H](CC(=O)O)C(=O)N[C@@H](CC(=O)O)C(=O)N[C@@H](CS)C(=O)N[C@H](C(=O)N[C@@H](CC(N)=O)C(=O)N[C@@H](Cc1ccc(O)cc1)C(=O)NCC(=O)N[C@@H](CC(N)=O)C(=O)N[C@@H](CS)C(=O)N[C@@H](CCCCN)C(=O)N[C@H](C(=O)N[C@@H](CC(C)C)C(=O)N[C@@H](CCCCN)C(=O)N[C@@H](CC(C)C)C(=O)N[C@@H](CCSC)C(=O)O)[C@@H](C)O)C(C)C)[C@@H](C)CC)C(C)C)C(C)C)C(C)C)[C@@H](C)CC)C(C)C)[C@@H](C)O)[C@@H](C)O)C(C)C)[C@@H](C)O)[C@@H](C)O)C(C)C
Representation class

How the current release can interpret this identity chemically.

map backed
Parent-residue sequence

Residue string used for positional interpretation when available.

MFTLKKSLFLVLILGMVSLSLCQQESNADKETTKEVTGEANTAGNVEIVEVAEVEKEMEELYKEIDDCVNYGNCKTLKLM
HELM

Polymer notation for modified peptide representation when available.

MFTLKKSLFLVLILGMVSLSLCQQESNADKETTKEVTGEANTAGNVEIVEVAEVEKEMEELYKEIDDCVNYGNCKTLKLM
SMILES

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

CC[C@H](C)[C@H](NC(=O)[C@H](CC(C)C)NC(=O)[C@@H](NC(=O)[C@H](CC(C)C)NC(=O)[C@H](Cc1ccccc1)NC(=O)[C@H](CC(C)C)NC(=O)[C@H](CO)NC(=O)[C@H](CCCCN)NC(=O)[C@H](CCCCN)NC(=O)[C@H](CC(C)C)NC(=O)[C@@H](NC(=O)[C@H](Cc1ccccc1)NC(=O)[C@@H](N)CCSC)[C@@H](C)O)C(C)C)C(=O)N[C@@H](CC(C)C)C(=O)NCC(=O)N[C@@H](CCSC)C(=O)N[C@H](C(=O)N[C@@H](CO)C(=O)N[C@@H](CC(C)C)C(=O)N[C@@H](CO)C(=O)N[C@@H](CC(C)C)C(=O)N[C@@H](CS)C(=O)N[C@@H](CCC(N)=O)C(=O)N[C@@H](CCC(N)=O)C(=O)N[C@@H](CCC(=O)O)C(=O)N[C@@H](CO)C(=O)N[C@@H](CC(N)=O)C(=O)N[C@@H](C)C(=O)N[C@@H](CC(=O)O)C(=O)N[C@@H](CCCCN)C(=O)N[C@@H](CCC(=O)O)C(=O)N[C@H](C(=O)N[C@H](C(=O)N[C@@H](CCCCN)C(=O)N[C@@H](CCC(=O)O)C(=O)N[C@H](C(=O)N[C@H](C(=O)NCC(=O)N[C@@H](CCC(=O)O)C(=O)N[C@@H](C)C(=O)N[C@@H](CC(N)=O)C(=O)N[C@H](C(=O)N[C@@H](C)C(=O)NCC(=O)N[C@@H](CC(N)=O)C(=O)N[C@H](C(=O)N[C@@H](CCC(=O)O)C(=O)N[C@H](C(=O)N[C@H](C(=O)N[C@@H](CCC(=O)O)C(=O)N[C@H](C(=O)N[C@@H](C)C(=O)N[C@@H](CCC(=O)O)C(=O)N[C@H](C(=O)N[C@@H](CCC(=O)O)C(=O)N[C@@H](CCCCN)C(=O)N[C@@H](CCC(=O)O)C(=O)N[C@@H](CCSC)C(=O)N[C@@H](CCC(=O)O)C(=O)N[C@@H](CCC(=O)O)C(=O)N[C@@H](CC(C)C)C(=O)N[C@@H](Cc1ccc(O)cc1)C(=O)N[C@@H](CCCCN)C(=O)N[C@@H](CCC(=O)O)C(=O)N[C@H](C(=O)N[C@@H](CC(=O)O)C(=O)N[C@@H](CC(=O)O)C(=O)N[C@@H](CS)C(=O)N[C@H](C(=O)N[C@@H](CC(N)=O)C(=O)N[C@@H](Cc1ccc(O)cc1)C(=O)NCC(=O)N[C@@H](CC(N)=O)C(=O)N[C@@H](CS)C(=O)N[C@@H](CCCCN)C(=O)N[C@H](C(=O)N[C@@H](CC(C)C)C(=O)N[C@@H](CCCCN)C(=O)N[C@@H](CC(C)C)C(=O)N[C@@H](CCSC)C(=O)O)[C@@H](C)O)C(C)C)[C@@H](C)CC)C(C)C)C(C)C)C(C)C)[C@@H](C)CC)C(C)C)[C@@H](C)O)[C@@H](C)O)C(C)C)[C@@H](C)O)[C@@H](C)O)C(C)C
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 & modifications1 signal
FeaturePositionsInterpretationLink
Form-level topologyATLPF0028958Open-chain form. Residue-level connection endpoints are shown separately when available.Not linked
02

Physicochemical profile

10 descriptors

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

·
Core descriptors80 aa · pI 4.1 · GRAVY -0.09
Length
80 aa
Monoisotopic mass
8945.44 Da
Average mass
8951.33 Da
Net charge at pH 7.4
-7.00
Estimated pI
4.14
GRAVY
-0.085
KD-positive residues
42.5%
Aromatic residues
5.0%
Developability interpretation
Ionization context
pH 7.4 separated from pI
Hydrophobicity balance
Leans hydrophilic
Amphipathic moment (μH)
0.68
Computation boundary
Standard-sequence only
Charge & residue composition
pH charge context

Modeled net charge across common formulation and assay pH checkpoints.

pH 2
8.84
pH 5
-5.40
pH 6
-6.84
pH 7.4
-7.28
pH 9
-10.27
pH 12
-20.50
Residue-class composition

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

Acidic (D,E)
15 · 18.8%
Basic (K,R,H)
8 · 10.0%
Polar uncharged (N,Q,S,T)
17 · 21.3%
Hydrophobic aliphatic (A,V,I,L,M)
29 · 36.3%
Aromatic (F,W,Y)
4 · 5.0%
Conformational / sulfur (G,P,C)
7 · 8.8%
Top residues
E1215.0%L1012.5%K810.0%V810.0%T67.5%N56.3%A45.0%G45.0%
Hydropathy & amphipathic windows
Hydropathy windows

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

Most hydrophobic window
8-14
LFLVLIL
GRAVY 3.814
Most hydrophilic window
29-35
DKETTKE
GRAVY -2.814
74 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
59-70
EELYKEIDDCVN
μH 2.27 · charge -4.0
12 aa window
58-69
MEELYKEIDDCV
μH 2.15 · charge -4.0
12 aa window
60-71
ELYKEIDDCVNY
μH 2.12 · charge -3.0
15 aa window
56-70
KEMEELYKEIDDCVN
μH 2.11 · charge -4.0
18 aa window
53-70
EVEKEMEELYKEIDDCVN
μH 2.05 · charge -6.0
Sequence-liability cues
Sequence-liability notes

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

Asn deamidation motif
NT · pos 41
Asn followed by small/polar residues is a known sequence context to review for deamidation susceptibility.
Oxidation-sensitive residues
M, C · pos 1, 16, 22, 58, 68, 74 +1
Met, Trp, and Cys residues can merit formulation review for oxidation or covalent-state sensitivity.
Cys covalent complexity
C · pos 22, 68, 74
Multiple cysteines can indicate disulfide or free-thiol interpretation requirements.
Alpha-helix amphipathic projection
Helical wheel · Edmundson projection
μH = 0.68100°/residue · 80 aa
μH1: M (Met) · Hydrophobic · K-D 1.9M12: F (Phe) · Aromatic · K-D 2.8F3: T (Thr) · Polar · K-D -0.7T4: L (Leu) · Hydrophobic · K-D 3.8L5: K (Lys) · Basic + · K-D -3.9K56: K (Lys) · Basic + · K-D -3.9K7: S (Ser) · Polar · K-D -0.8S8: L (Leu) · Hydrophobic · K-D 3.8L9: F (Phe) · Aromatic · K-D 2.8F10: L (Leu) · Hydrophobic · K-D 3.8L1011: V (Val) · Hydrophobic · K-D 4.2V12: L (Leu) · Hydrophobic · K-D 3.8L13: I (Ile) · Hydrophobic · K-D 4.5I14: L (Leu) · Hydrophobic · K-D 3.8L15: G (Gly) · Special · K-D -0.4G1516: M (Met) · Hydrophobic · K-D 1.9M17: V (Val) · Hydrophobic · K-D 4.2V18: S (Ser) · Polar · K-D -0.8S19: L (Leu) · Hydrophobic · K-D 3.8L20: S (Ser) · Polar · K-D -0.8S2021: L (Leu) · Hydrophobic · K-D 3.8L22: C (Cys) · Special · K-D 2.5C23: Q (Gln) · Polar · K-D -3.5Q24: Q (Gln) · Polar · K-D -3.5Q25: E (Glu) · Acidic − · K-D -3.5E2526: S (Ser) · Polar · K-D -0.8S27: N (Asn) · Polar · K-D -3.5N28: A (Ala) · Hydrophobic · K-D 1.8A29: D (Asp) · Acidic − · K-D -3.5D30: K (Lys) · Basic + · K-D -3.9K3031: E (Glu) · Acidic − · K-D -3.5E32: T (Thr) · Polar · K-D -0.7T33: T (Thr) · Polar · K-D -0.7T34: K (Lys) · Basic + · K-D -3.9K35: E (Glu) · Acidic − · K-D -3.5E3536: V (Val) · Hydrophobic · K-D 4.2V37: T (Thr) · Polar · K-D -0.7T38: G (Gly) · Special · K-D -0.4G39: E (Glu) · Acidic − · K-D -3.5E40: A (Ala) · Hydrophobic · K-D 1.8A4041: N (Asn) · Polar · K-D -3.5N42: T (Thr) · Polar · K-D -0.7T43: A (Ala) · Hydrophobic · K-D 1.8A44: G (Gly) · Special · K-D -0.4G45: N (Asn) · Polar · K-D -3.5N4546: V (Val) · Hydrophobic · K-D 4.2V47: E (Glu) · Acidic − · K-D -3.5E48: I (Ile) · Hydrophobic · K-D 4.5I49: V (Val) · Hydrophobic · K-D 4.2V50: E (Glu) · Acidic − · K-D -3.5E5051: V (Val) · Hydrophobic · K-D 4.2V52: A (Ala) · Hydrophobic · K-D 1.8A53: E (Glu) · Acidic − · K-D -3.5E54: V (Val) · Hydrophobic · K-D 4.2V55: E (Glu) · Acidic − · K-D -3.5E5556: K (Lys) · Basic + · K-D -3.9K57: E (Glu) · Acidic − · K-D -3.5E58: M (Met) · Hydrophobic · K-D 1.9M59: E (Glu) · Acidic − · K-D -3.5E60: E (Glu) · Acidic − · K-D -3.5E6061: L (Leu) · Hydrophobic · K-D 3.8L62: Y (Tyr) · Aromatic · K-D -1.3Y63: K (Lys) · Basic + · K-D -3.9K64: E (Glu) · Acidic − · K-D -3.5E65: I (Ile) · Hydrophobic · K-D 4.5I6566: D (Asp) · Acidic − · K-D -3.5D67: D (Asp) · Acidic − · K-D -3.5D68: C (Cys) · Special · K-D 2.5C69: V (Val) · Hydrophobic · K-D 4.2V70: N (Asn) · Polar · K-D -3.5N7071: Y (Tyr) · Aromatic · K-D -1.3Y72: G (Gly) · Special · K-D -0.4G73: N (Asn) · Polar · K-D -3.5N74: C (Cys) · Special · K-D 2.5C75: K (Lys) · Basic + · K-D -3.9K7576: T (Thr) · Polar · K-D -0.7T77: L (Leu) · Hydrophobic · K-D 3.8L78: K (Lys) · Basic + · K-D -3.9K79: L (Leu) · Hydrophobic · K-D 3.8L80: M (Met) · Hydrophobic · K-D 1.9M80
Hydrophobic moment0.68
Mean K-D hydropathy-0.09
Approx. net charge-7
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
97.38
Instability index
12.5

At or below 40 — predicted stable in vitro.

Boman index
1.24 kcal/mol
Molar extinction coefficient (280 nm)
2,980 M⁻¹·cm⁻¹

A280 (1 g/L) ≈ 0.33 · 3,105 M⁻¹·cm⁻¹ with 1 disulfide

Structure-derived (developability)

Computed from the representative peptidoform's chemical structure. Rule-of-5 / beyond-Ro5 framing per Lipinski/Doak.

Topological polar surface area
3674.3 Ų
Computed logP (Crippen)
-33.67

Computed logP — distinct from the measured logD endpoint.

Hydrogen-bond donors
126
Hydrogen-bond acceptors
130
Rotatable bonds
316
Rule-of-5 / beyond-Ro5 flags
Beyond bRo5

3 Ro5 violations · MW 8,951.39 Da

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
ATLPC0026628
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/ATLPC0026628
open
curl -sS 'https://admetatlas.scbdd.com/api/v1/peptides/ATLPC0026628' \
  -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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