Peptide·plain sequence-like
Bivalirudin
ATLPC0035832
FPRPGGGGNGDFEEIPEEYL
- Length20 aa
- Monoisotopic mass
ATLPC0035832
FPRPGGGGNGDFEEIPEEYL
Reviewed sequence, HELM, or SMILES representation used to interpret this peptide identity.
Molecular graph, chemical representation, 3D references, and covalent topology when available.
Computed sequence-derived descriptors and any measured physicochemical evidence such as lipophilicity.
Product-level route, label, and clinical context that frames peptide-level evidence.
Cross-domain evidence distribution, traceability, and measurement-level detail for this peptide.
Reference-level support for checking reported names, sequence notation, and peptide identity agreement.
Stable record access, analysis-ready files, and scripted retrieval for reproducing this profile view.
Are molecular graph, topology, or 3D coordinates available?
What evidence describes systemic exposure or absorption?
What is known about distribution, binding, permeability, or barrier crossing?
How stable is the peptide in biological matrices or protease systems?
What evidence describes clearance or persistence?
What safety, toxicity, or tolerability evidence is attached?
Can every measurement be reviewed in one cross-domain table?
Can the peptide identity be checked against reported names, sequence notation, and reference links?
Normalized for positional visualization, not a replacement for the reported modified notation.
FPRPGGGGNGDFEEIPEEYL
Original notation retained for interpretation and comparison.
FPRPGGGGNGDFEEIPEEYL
Interpretation: Evidence should be compared across compatible peptide identities and peptidoforms. A sequence-only match may not be equivalent when terminal modifications, stereochemistry, cyclization, or cross-links differ.
FPRPGGGGNGDFEEIPEEYLPolymer notation for modified peptide representation when available.
Not availableChemical graph string used for atom-level 2D depiction when available.
Not availableA 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.
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.
No disulfide, staple, coordination, other cross-link, or residue-level modification annotation is attached to this peptide in the current release.
Interpretation: A 2D graph describes connectivity, not conformation. A 3D reference describes one coordinate model or solved state, not the full ensemble. ADMET interpretation should account for peptidoform, topology, and assay context together.
Modeled net charge across common formulation and assay pH checkpoints.
Seven-residue sliding windows expose local patches hidden by whole-sequence GRAVY.
Top alpha-helix hydrophobic-moment windows across 12, 15, 18, and 21 residues.
Motifs are review prompts for formulation or CMC interpretation; they are not degradation predictions.
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.
A280 (1 g/L) ≈ 0.68
Computed from the representative peptidoform's chemical structure. Rule-of-5 / beyond-Ro5 framing per Lipinski/Doak.
Computed logP — distinct from the measured logD endpoint.
Identity, sequence, profile-level fields, and current release view metadata.
The request returns the same structured peptide record used by this profile. Measurement downloads use the same peptide identifier and public release visibility.
curl -sS 'https://admetatlas.scbdd.com/api/v1/peptides/ATLPC0035832' \
-H 'accept: application/json' \
-H 'X-Visibility: public_release'Interpretation: Use these files as the reproducible data package for this peptide profile. Cross-peptide comparison still depends on compatible endpoints, assays, species or model systems, route, dose, matrix, and evidence layer.
Features are shown only when a reported notation or topology record supports them.
Grouped composition is often more interpretable than a long amino-acid list.
The projection assumes an α-helix conformation; a long μH arrow indicates an amphipathic helix, common in antimicrobial peptides.
3 Ro5 violations · MW 2,180.32 Da
Endpoint-level measurements attached to this peptide, suitable for review or reanalysis.
Nested peptide record for scripted retrieval, including identity and evidence context.