Peptide·plain sequence-like

Angiotensin II

ATLPC0035835

DRVYIHPF

Routes

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Length
8 aa
Monoisotopic mass
1045.5 Da
Net charge @ pH 7.4
0.10
Isoelectric point
7.54
GRAVY
-0.325

Coveragecounts only · not riskATLPC0035835

Measurements
0
Endpoints
0
Domains
0/5
Products
1

No matrix stability evidence
No clearance evidence
Product-level review pending
No sequence liability cues

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

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: 8
Peptidoform features: 0
Documented molecular forms: 1
Representations: 2

Documented molecular forms1 form linked to this peptide identity

Form	Topology	Modifications	Connections	Representations	Measurements
ATLPF0038977	—	4	—	1	—

Residue view

Residue display

8 residues

D1R2V3Y4I5H6P7F8

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.

DRVYIHPF

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 & modifications1 signal

Feature	Positions	Interpretation	Link
Form-level topology	ATLPF0038977	Open-chain form. Residue-level connection endpoints are shown separately when available.	Not linked

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 descriptors8 aa · pI 7.5 · GRAVY -0.33

Length: 8 aa
Monoisotopic mass: 1045.53 Da
Average mass: 1046.19 Da
Net charge at pH 7.4: 0.10
Estimated pI: 7.54
GRAVY: -0.325
KD-positive residues: 37.5%
Aromatic residues: 25.0%

Developability interpretation

Ionization context: pH 7.4 close to pI
Hydrophobicity balance: Leans hydrophilic
Amphipathic moment (μH): 0.50
Computation boundary: Standard-sequence only

Charge & residue composition

pH charge context

Modeled net charge across common formulation and assay pH checkpoints.

pH 2

2.96

pH 5

1.08

pH 6

0.77

pH 7.4

0.05

pH 9

-0.79

pH 12

-2.23

Residue-class composition

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

Acidic (D,E)

1 · 12.5%

Basic (K,R,H)

2 · 25.0%

Hydrophobic aliphatic (A,V,I,L,M)

2 · 25.0%

Aromatic (F,W,Y)

2 · 25.0%

Conformational / sulfur (G,P,C)

1 · 12.5%

Top residues

R112.5%D112.5%H112.5%I112.5%F112.5%P112.5%Y112.5%V112.5%

Hydropathy & amphipathic windows

Hydropathy windows

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

Most hydrophobic window

2-8

RVYIHPF

GRAVY 0.129

Most hydrophilic window

1-7

DRVYIHP

GRAVY -0.771

2 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.

Sequence is shorter than the local amphipathic-window sizes used here.

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

μ_H = 0.50100°/residue · 8 aa

Hydrophobic moment0.50

Mean K-D hydropathy-0.33

Approx. net charge0

Projection angle100° / residue

The pale sector marks the direction of the hydrophobic face inferred from μ_H. This is a projection assumption, not a measured fold.

HydrophobicAromaticPolarBasic +Acidic −Specialhydrophobic faceμ_H arrow → hydrophobic face

The projection assumes an α-helix conformation; a long μ_H 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

85.00

Instability index

25.8

At or below 40 — predicted stable in vitro.

Boman index

2.06 kcal/mol

Molar extinction coefficient (280 nm)

1,490 M⁻¹·cm⁻¹

A280 (1 g/L) ≈ 1.42

Structure-derived (developability)

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

Topological polar surface area

408.8 Å²

Computed logP (Crippen)

-1.31

Computed logP — distinct from the measured logD endpoint.

Hydrogen-bond donors

Hydrogen-bond acceptors

Rotatable bonds

Rule-of-5 / beyond-Ro5 flags

Beyond bRo5

3 Ro5 violations · MW 1,046.2 Da

Product context

1 products

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

Summary1 linked product

Linked products: 1
Label context: None
Clinical trials: 30
Safety label cues: None

Linked products1 shown

Angiotensin II

Peptide-product match

Reviewed peptide match

Route / product class

intravenous · Injection, solution

Clinical context

30 trial records · 2 exact intervention matches · 6 with results · latest 2026-04-24

Label safety context

No label safety cue linked

View product

Data access & reproducibility

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

Record scopePublic release

ATL peptide ID: ATLPC0035835
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/ATLPC0035835

open

curl -sS 'https://admetatlas.scbdd.com/api/v1/peptides/ATLPC0035835' \
  -H 'accept: application/json' \
  -H 'X-Visibility: public_release'

Form

Topology

Modifications

Connections

Representations

Measurements

ATLPF0038977

—

Feature

Positions

Interpretation

Link

Form-level topology

ATLPF0038977

Open-chain form. Residue-level connection endpoints are shown separately when available.

Not linked

Angiotensin II