Peptide·map backed
ATLPC0035489
ATLPC0035489
MQIFVKTLTGKTITLEVEPSDTIENVKAKIQDKEGIPPDQQRLIFAGKQLEDGRTLSDYNIQKESTLHLVLRLR
- Length74 aa
- Monoisotopic mass8445.6 Da
Stack
ATLPC0035489
MQIFVKTLTGKTITLEVEPSDTIENVKAKIQDKEGIPPDQQRLIFAGKQLEDGRTLSDYNIQKESTLHLVLRLR
Is the peptide identity interpretable at sequence or structure-string level?
Are molecular graph, topology, or 3D coordinates available?
Can basic developability descriptors be computed?
Is this peptide linked to approved or named product context?
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?
Can this profile view be reproduced from structured records?
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.
Features are shown only when a reported notation or topology record supports them.
Polymer notation suitable for modified peptide and conjugate representation when available.
MQIFVKTLTGKTITLEVEPSDTIENVKAKIQDKEGIPPDQQRLIFAGKQLEDGRTLSDYNIQKESTLHLVLRLR
Chemical graph representation for chemistry-aware interpretation when available.
CC[C@H](C)[C@H](NC(=O)[C@H](CC(C)C)NC(=O)[C@H](CCCNC(=N)N)NC(=O)[C@H](CCC(N)=O)NC(=O)[C@H](CCC(N)=O)NC(=O)[C@H](CC(=O)O)NC(=O)[C@@H]1CCCN1C(=O)[C@@H]1CCCN1C(=O)[C@@H](NC(=O)CNC(=O)[C@H](CCC(=O)O)NC(=O)[C@H](CCCCN)NC(=O)[C@H](CC(=O)O)NC(=O)[C@H](CCC(N)=O)NC(=O)[C@@H](NC(=O)[C@H](CCCCN)NC(=O)[C@H](C)NC(=O)[C@H](CCCCN)NC(=O)[C@@H](NC(=O)[C@H](CC(N)=O)NC(=O)[C@H](CCC(=O)O)NC(=O)[C@@H](NC(=O)[C@@H](NC(=O)[C@H](CC(=O)O)NC(=O)[C@H](CO)NC(=O)[C@@H]1CCCN1C(=O)[C@H](CCC(=O)O)NC(=O)[C@@H](NC(=O)[C@H](CCC(=O)O)NC(=O)[C@H](CC(C)C)NC(=O)[C@@H](NC(=O)[C@@H](NC(=O)[C@@H](NC(=O)[C@H](CCCCN)NC(=O)CNC(=O)[C@@H](NC(=O)[C@H](CC(C)C)NC(=O)[C@@H](NC(=O)[C@H](CCCCN)NC(=O)[C@@H](NC(=O)[C@H](Cc1ccccc1)NC(=O)[C@@H](NC(=O)[C@H](CCC(N)=O)NC(=O)[C@@H](N)CCSC)[C@@H](C)CC)C(C)C)[C@@H](C)O)[C@@H](C)O)[C@@H](C)O)[C@@H](C)CC)[C@@H](C)O)C(C)C)[C@@H](C)O)[C@@H](C)CC)C(C)C)[C@@H](C)CC)[C@@H](C)CC)C(=O)N[C@@H](Cc1ccccc1)C(=O)N[C@@H](C)C(=O)NCC(=O)N[C@@H](CCCCN)C(=O)N[C@@H](CCC(N)=O)C(=O)N[C@@H](CC(C)C)C(=O)N[C@@H](CCC(=O)O)C(=O)N[C@@H](CC(=O)O)C(=O)NCC(=O)N[C@@H](CCCNC(=N)N)C(=O)N[C@H](C(=O)N[C@@H](CC(C)C)C(=O)N[C@@H](CO)C(=O)N[C@@H](CC(=O)O)C(=O)N[C@@H](Cc1ccc(O)cc1)C(=O)N[C@@H](CC(N)=O)C(=O)N[C@H](C(=O)N[C@@H](CCC(N)=O)C(=O)N[C@@H](CCCCN)C(=O)N[C@@H](CCC(=O)O)C(=O)N[C@@H](CO)C(=O)N[C@H](C(=O)N[C@@H](CC(C)C)C(=O)N[C@@H](Cc1c[nH]cn1)C(=O)N[C@@H](CC(C)C)C(=O)N[C@H](C(=O)N[C@@H](CC(C)C)C(=O)N[C@@H](CCCNC(=N)N)C(=O)N[C@@H](CC(C)C)C(=O)N[C@@H](CCCNC(=N)N)C(=O)O)C(C)C)[C@@H](C)O)[C@@H](C)CC)[C@@H](C)O
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.Sequence > 30 aa — only termini and every fifth position are numbered because later turns share earlier wheel angles.
3 Ro5 violations · MW 8,450.77 Da
Endpoint-level measurements attached to this peptide, suitable for review or reanalysis.
Nested peptide record for scripted retrieval, including identity and evidence context.