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Peptide·plain sequence-like

Salmon Calcitonin

ATLPC0001542

CSNLSTCVLGKLSQELHKLQTYPRTNTGSGTP

Routes
Compare in workbenchDownload releaseAPI JSON
  • Length
    32 aa
  • Monoisotopic mass
    3432.7 Da
  • Net charge @ pH 7.4
    2.10
  • Isoelectric point
    8.80
  • GRAVY
    -0.538
On this page
  • 01 Sequence & molecular identity
  • 02 Physicochemical profile
  • 03 Exposure / Absorption
  • 04 Distribution / Barrier
  • 05 Excretion / Persistence
  • 06 Evidence landscape
  • 07 Product context
  • 08 Identity & reference map
  • 09 Data access & reproducibility
Coveragecounts only · not riskATLPC0001542
  • Measurements
    30
  • Endpoints
    8
  • Domains
    3/5
  • Products
    1
  • No matrix stability evidence
  • 3 clearance measurements
  • Product-level review pending
  • 3 liability motifs
Jump to domain

Open the matching evidence section below

All evidence index · 30
Exposure / Absorption
22 measurements
Distribution / Barrier
5 measurements
Metabolic & Proteolytic Stability
No evidence
Excretion / Persistence
3 measurements
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
32
Peptidoform features
0
Documented molecular forms
1
Representations
2
Documented molecular forms1 form linked to this peptide identity
FormTopologyModificationsConnectionsRepresentationsMeasurements
ATLPF0001710———Notation only2
Residue view
Residue display
32 residues
C1S2N3L4S5T6C7V8L9G10K11L12S13Q14E15L16H17K18L19Q20T21Y22P23R24T25N26T27G28S29G30T31P32
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.

CSNLSTCVLGKLSQELHKLQTYPRTNTGSGTP
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 references8 references
Structure reference·
3D coordinates·Sequence matchexperimental
Sequence match·reference selected·identity 100.0%·confidence experimental
LinkMethodConfidenceMatch
OpenSequence matchexperimental100.0% identity
OpenSequence matchexperimental100.0% identity
OpenSequence matchexperimental100.0% identity
OpenSequence matchexperimental100.0% identity
OpenSequence matchexperimental100.0% identity
OpenSequence matchexperimental100.0% identity
OpenSequence matchexperimental100.0% identity
OpenSequence matchexperimental100.0% identity
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 descriptors32 aa · pI 8.8 · GRAVY -0.54
Length
32 aa
Monoisotopic mass
3432.71 Da
Average mass
3434.89 Da
Net charge at pH 7.4
2.10
Estimated pI
8.80
GRAVY
-0.538
KD-positive residues
25.0%
Aromatic residues
3.1%
Developability interpretation
Ionization context
pH 7.4 separated from pI
Hydrophobicity balance
Leans hydrophilic
Amphipathic moment (μH)
0.83
Computation boundary
Standard-sequence only
Charge & residue composition
pH charge context

Modeled net charge across common formulation and assay pH checkpoints.

pH 2
4.97
pH 5
3.12
pH 6
2.77
pH 7.4
1.90
pH 9
-0.34
pH 12
-4.11
Residue-class composition

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

Acidic (D,E)
1 · 3.1%
Basic (K,R,H)
4 · 12.5%
Polar uncharged (N,Q,S,T)
13 · 40.6%
Hydrophobic aliphatic (A,V,I,L,M)
6 · 18.8%
Aromatic (F,W,Y)
1 · 3.1%
Conformational / sulfur (G,P,C)
7 · 21.9%
Top residues
L515.6%T515.6%S412.5%G39.4%N26.3%C26.3%Q26.3%K26.3%
Hydropathy & amphipathic windows
Hydropathy windows

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

Most hydrophobic window
4-10
LSTCVLG
GRAVY 1.771
Most hydrophilic window
20-26
QTYPRTN
GRAVY -2.257
26 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
8-19
VLGKLSQELHKL
μH 2.06 · charge 1.1
12 aa window
9-20
LGKLSQELHKLQ
μH 1.75 · charge 1.1
12 aa window
7-18
CVLGKLSQELHK
μH 1.64 · charge 1.1
15 aa window
8-22
VLGKLSQELHKLQTY
μH 1.59 · charge 1.1
12 aa window
10-21
GKLSQELHKLQT
μH 1.55 · charge 1.1
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 26
Asn followed by small/polar residues is a known sequence context to review for deamidation susceptibility.
Oxidation-sensitive residues
C · pos 1, 7
Met, Trp, and Cys residues can merit formulation review for oxidation or covalent-state sensitivity.
Cys covalent complexity
C · pos 1, 7
Multiple cysteines can indicate disulfide or free-thiol interpretation requirements.
Alpha-helix amphipathic projection
Helical wheel · Edmundson projection
μH = 0.83100°/residue · 32 aa
μH1: C (Cys) · Special · K-D 2.5C12: S (Ser) · Polar · K-D -0.8S3: N (Asn) · Polar · K-D -3.5N4: L (Leu) · Hydrophobic · K-D 3.8L5: S (Ser) · Polar · K-D -0.8S56: T (Thr) · Polar · K-D -0.7T7: C (Cys) · Special · K-D 2.5C8: V (Val) · Hydrophobic · K-D 4.2V9: L (Leu) · Hydrophobic · K-D 3.8L10: G (Gly) · Special · K-D -0.4G1011: K (Lys) · Basic + · K-D -3.9K12: L (Leu) · Hydrophobic · K-D 3.8L13: S (Ser) · Polar · K-D -0.8S14: Q (Gln) · Polar · K-D -3.5Q15: E (Glu) · Acidic − · K-D -3.5E1516: L (Leu) · Hydrophobic · K-D 3.8L17: H (His) · Basic + · K-D -3.2H18: K (Lys) · Basic + · K-D -3.9K19: L (Leu) · Hydrophobic · K-D 3.8L20: Q (Gln) · Polar · K-D -3.5Q2021: T (Thr) · Polar · K-D -0.7T22: Y (Tyr) · Aromatic · K-D -1.3Y23: P (Pro) · Special · K-D -1.6P24: R (Arg) · Basic + · K-D -4.5R25: T (Thr) · Polar · K-D -0.7T2526: N (Asn) · Polar · K-D -3.5N27: T (Thr) · Polar · K-D -0.7T28: G (Gly) · Special · K-D -0.4G29: S (Ser) · Polar · K-D -0.8S30: G (Gly) · Special · K-D -0.4G3031: T (Thr) · Polar · K-D -0.7T32: P (Pro) · Special · K-D -1.6P32
Hydrophobic moment0.83
Mean K-D hydropathy-0.54
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.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
70.00
Instability index
17.8

At or below 40 — predicted stable in vitro.

Boman index
1.70 kcal/mol
Molar extinction coefficient (280 nm)
1,490 M⁻¹·cm⁻¹

A280 (1 g/L) ≈ 0.43 · 1,615 M⁻¹·cm⁻¹ with 1 disulfide

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

Exposure / Absorption

22 records

What evidence describes systemic exposure or absorption?

Evidence records
22
Complete canonical measurements and observations attached to this domain.
Endpoint scope
4
Formal ADMET endpoints represented for this peptide.
Matched-context in preview
11
Quantitative results that may be analysed only with scientifically compatible records.
Reported results in preview
3
Qualitative, narrative, or review-first results interpreted in their source context.
Endpoints in scopeBioavailabilityAUCCmaxTmax
Loading 22 Exposure / Absorption records…
04

Distribution / Barrier

5 records

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

Evidence records
5
Complete canonical measurements and observations attached to this domain.
Endpoint scope
2
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
1
Qualitative, narrative, or review-first results interpreted in their source context.
Endpoints in scopePlasma protein bindingVd
Loading 5 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
0

barrier evidence

05

Excretion / Persistence

3 records

What evidence describes clearance or persistence?

Evidence records
3
Complete canonical measurements and observations attached to this domain.
Endpoint scope
2
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
0
Qualitative, narrative, or review-first results interpreted in their source context.
Endpoints in scopeHalf LifeClearance
Loading 3 Excretion / Persistence records…
06

Evidence landscape

30 records

Cross-domain evidence distribution and measurement-level detail. 20 of 30 evidence records are included in the profile preview; the full index is loaded below.

Loading 30 measurements…
07

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
1
Clinical trials
51
Safety label cues
None
Linked products1 shown

Salmon Calcitonin

sCT (Salmon calcitonin)sCT
Peptide-product match
Reviewed peptide match
Route / product class
Subcutaneous or intramuscular Injection · Intranasal use · Bone Density Conservation Agents
Clinical context
51 trial records · 2 exact intervention matches · 10 with results · latest 2026-03-11
Label safety context
Label linked
View product
08

Identity & reference map

30 sources

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

·
Summary8 reference groups
Identity type
canonical sequence
Reported notation
1
Reference groups
8
Measurements
30
ATL peptide ID
ATLPC0001542
Identity concordance
Identity concordance
Exact reported notation

Reported sequence string matches the current peptide notation.

0 / 30
Parent-residue compatible

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

0 / 30
Different notation

Reported notation does not resolve to the current display sequence.

4 / 30
Source sequence not captured

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

26 / 30
Reported sequence notation
Different4 references
CSNLSTCVLGKLSQELHKLQTYPRTNTGSGTP-NH2
Current identity
CSNLSTCVLGKLSQELHKLQTYPRTNTGSGTP
Reported names
No distinct human-readable aliases are exposed.
Reference map8 reference groups
Reference map

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

ReferenceSupportsReported identityRecords
Reference
Open
Exposure
Area Under Curve, Max Concentration
No reported alias
14 identity
11 evidence
Source record
Open
DistributionExposure
Bioavailability, Plasma Protein Binding
No reported alias
CSNLSTCVLGKLSQELHKLQTYPRTNTGSGTP-NH2different
4 identity
4 evidence
Reference
Open
Persistence
Half Life
No reported alias
2 identity
2 evidence
Reference
Open
Distribution
Plasma Protein Binding, Volume Of Distribution
No reported alias
2 identity
2 evidence
Reference
Open
Identity only
No reported alias
4 identity
0 evidence
Reference
Open
Distribution
Volume Of Distribution
No reported alias
1 identity
1 evidence
Reference
Open
Identity only
No reported alias
2 identity
0 evidence
Reference
Open
Identity only
No reported alias
1 identity
0 evidence
09

Data access & reproducibility

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

·
Record scopePublic release
ATL peptide ID
ATLPC0001542
Identity type
canonical sequence
ADMET endpoints
8
Evidence records
30
Reference groups
8
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/ATLPC0001542
open
curl -sS 'https://admetatlas.scbdd.com/api/v1/peptides/ATLPC0001542' \
  -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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