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Peptide·plain sequence-like

ATLPC0011617

ATLPC0011617

TFFYGGSRGRRNNFRTEEY

Routes
Compare in workbenchDownload releaseAPI JSON
  • Length
    19 aa
  • Monoisotopic mass
    2356.1 Da
  • Net charge @ pH 7.4
    2.00
  • Isoelectric point
    10.11
  • GRAVY
    -1.558
On this page
  • 01 Sequence & molecular identity
  • 02 Physicochemical profile
  • 03 Distribution / Barrier
  • 04 Evidence landscape
  • 05 Product context
  • 06 Identity & reference map
  • 07 Data access & reproducibility
Coveragecounts only · not riskATLPC0011617
  • Measurements
    24
  • Endpoints
    1
  • Domains
    1/5
  • Products
    —
  • No matrix stability evidence
  • No clearance evidence
  • No immunogenicity context
  • No sequence liability cues
Jump to domain

Open the matching evidence section below

All evidence index · 24
Exposure / Absorption
No evidence
Distribution / Barrier
24 measurements
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 summaryCanonical sequence only
Identity status
Canonical sequence only
Residues
19
Peptidoform features
0
Documented molecular forms
1
Representations
2
Documented molecular forms1 form linked to this peptide identity
FormTopologyModificationsConnectionsRepresentationsMeasurements
ATLPF0012731———Notation only—
Residue view
Residue display
19 residues
T1F2F3Y4G5G6S7R8G9R10R11N12N13F14R15T16E17E18Y19
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.

TFFYGGSRGRRNNFRTEEY
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·PEPstrMOD predictionpredicted
PEPstrMOD prediction·reference selected·length 19 aa·confidence predicted
LinkMethodConfidenceMatch
OpenPEPstrMOD modelpredicted19 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 descriptors19 aa · pI 10.1 · GRAVY -1.56
Length
19 aa
Monoisotopic mass
2356.11 Da
Average mass
2357.53 Da
Net charge at pH 7.4
2.00
Estimated pI
10.11
GRAVY
-1.558
KD-positive residues
15.8%
Aromatic residues
26.3%
Developability interpretation
Ionization context
pH 7.4 separated from pI
Hydrophobicity balance
Leans hydrophilic
Amphipathic moment (μH)
0.63
Computation boundary
Standard-sequence only
Charge & residue composition
pH charge context

Modeled net charge across common formulation and assay pH checkpoints.

pH 2
4.96
pH 5
2.26
pH 6
2.03
pH 7.4
1.94
pH 9
1.14
pH 12
-1.94
Residue-class composition

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

Acidic (D,E)
2 · 10.5%
Basic (K,R,H)
4 · 21.1%
Polar uncharged (N,Q,S,T)
5 · 26.3%
Aromatic (F,W,Y)
5 · 26.3%
Conformational / sulfur (G,P,C)
3 · 15.8%
Top residues
R421.1%G315.8%F315.8%N210.5%E210.5%T210.5%Y210.5%S15.3%
Hydropathy & amphipathic windows
Hydropathy windows

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

Most hydrophobic window
1-7
TFFYGGS
GRAVY 0.286
Most hydrophilic window
7-13
SRGRRNN
GRAVY -3.100
13 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
TFFYGGSRGRRN
μH 0.91 · charge 3.0
15 aa window
1-15
TFFYGGSRGRRNNFR
μH 0.87 · charge 4.0
15 aa window
2-16
FFYGGSRGRRNNFRT
μH 0.83 · charge 4.0
12 aa window
4-15
YGGSRGRRNNFR
μH 0.73 · charge 4.0
12 aa window
5-16
GGSRGRRNNFRT
μH 0.66 · charge 4.0
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 = 0.63100°/residue · 19 aa
μH1: T (Thr) · Polar · K-D -0.7T12: F (Phe) · Aromatic · K-D 2.8F23: F (Phe) · Aromatic · K-D 2.8F34: Y (Tyr) · Aromatic · K-D -1.3Y45: G (Gly) · Special · K-D -0.4G56: G (Gly) · Special · K-D -0.4G67: S (Ser) · Polar · K-D -0.8S78: R (Arg) · Basic + · K-D -4.5R89: G (Gly) · Special · K-D -0.4G910: R (Arg) · Basic + · K-D -4.5R1011: R (Arg) · Basic + · K-D -4.5R1112: N (Asn) · Polar · K-D -3.5N1213: N (Asn) · Polar · K-D -3.5N1314: F (Phe) · Aromatic · K-D 2.8F1415: R (Arg) · Basic + · K-D -4.5R1516: T (Thr) · Polar · K-D -0.7T1617: E (Glu) · Acidic − · K-D -3.5E1718: E (Glu) · Acidic − · K-D -3.5E1819: Y (Tyr) · Aromatic · K-D -1.3Y19
Hydrophobic moment0.63
Mean K-D hydropathy-1.56
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
0.00
Instability index
96.8

Above 40 — predicted unstable in vitro.

Boman index
4.40 kcal/mol

Above 2.48 — elevated potential protein-binding.

Molar extinction coefficient (280 nm)
2,980 M⁻¹·cm⁻¹

A280 (1 g/L) ≈ 1.26

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

24 records

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

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
2
Quantitative results that may be analysed only with scientifically compatible records.
Reported results in preview
18
Qualitative, narrative, or review-first results interpreted in their source context.
Endpoints in scopeBBB penetration
Loading 24 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
20

barrier evidence

04

Evidence landscape

24 records

Cross-domain evidence distribution and measurement-level detail. 20 of 24 evidence records are included in the profile preview; the full index is loaded below.

Loading 24 measurements…
05

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
06

Identity & reference map

24 sources

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

·
Summary4 reference groups
Identity type
canonical sequence
Reported notation
1
Reference groups
4
Measurements
24
ATL peptide ID
ATLPC0011617
Identity concordance
Identity concordance
Exact reported notation

Reported sequence string matches the current peptide notation.

10 / 24
Parent-residue compatible

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

0 / 24
Different notation

Reported notation does not resolve to the current display sequence.

0 / 24
Source sequence not captured

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

14 / 24
Reported sequence notation
Exact10 references
TFFYGGSRGRRNNFRTEEY
Current identity
TFFYGGSRGRRNNFRTEEY
Reported names
brainpeps_observation_v2_152_20_37_14444a2bec8445eb93d4brainpeps_observation_v2_152_20_37_6771d7ba3993e55e6361brainpeps_observation_v2_152_20_38_86ea03a1c05418c137e8brainpeps_observation_v2_152_20_38_eec6e0db95cf3ff6caf4brainpeps_observation_v2_152_29_42_6cfdfee7370df3211863brainpeps_observation_v2_152_29_42_fcc6796ff754630e7217brainpeps_observation_v2_152_29_43_93d958648cbf6f5d7546brainpeps_observation_v2_152_29_43_fc74a49cd08a0bb56e8ebrainpeps_observation_v2_152_29_44_c6bf6d559b0b2f17baf8brainpeps_observation_v2_152_29_44_c8fe5db383a9f97cc802
Reference map4 reference groups
Reference map

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

ReferenceSupportsReported identityRecords
Reference
Open
Distribution
Blood Brain Barrier Penetration
brainpeps_observation_v2_152_20_37_14444a2bec8445eb93d4, brainpeps_observation_v2_152_20_38_eec6e0db95cf3ff6caf4, brainpeps_observation_v2_152_29_42_6cfdfee7370df3211863 +2 more
TFFYGGSRGRRNNFRTEEYexact
10 identity
8 evidence
Reference
Open
Distribution
Blood Brain Barrier Penetration
brainpeps_observation_v2_152_20_37_6771d7ba3993e55e6361, brainpeps_observation_v2_152_20_38_86ea03a1c05418c137e8, brainpeps_observation_v2_152_29_42_fcc6796ff754630e7217 +1 more
TFFYGGSRGRRNNFRTEEYexact
8 identity
7 evidence
Reference
Open
Distribution
Blood Brain Barrier Penetration
No reported alias
4 identity
4 evidence
Reference
Open
Distribution
Blood Brain Barrier Penetration
brainpeps_observation_v2_152_29_43_93d958648cbf6f5d7546
TFFYGGSRGRRNNFRTEEYexact
2 identity
1 evidence
07

Data access & reproducibility

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

·
Record scopePublic release
ATL peptide ID
ATLPC0011617
Identity type
canonical sequence
ADMET endpoints
1
Evidence records
24
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/ATLPC0011617
open
curl -sS 'https://admetatlas.scbdd.com/api/v1/peptides/ATLPC0011617' \
  -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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