dbacp04303
General Description
Peptide name : LTX-315
Source/Organism : Synthetic peptide
Linear/Cyclic : Linear
Chirality : L
Sequence Information
Sequence : KKWWKKW-Dip-K
Peptide length: Not available
C-terminal modification: Linear
N-terminal modification : Amidation
Non-natural peptide information: Dip : diphenylalanine
Activity Information
Assay type : MTT/MTS assay
Assay time : 30min
Activity : IC50 : 12.7 µM
Cell line : A375
Cancer type : Skin cancer
Other activity : Anti-microbial activity
Physicochemical Properties
Amino Acid Composition Bar Chart : Not available
Molecular mass : Not available
Aliphatic index : Not available
Instability index : Not available
Hydrophobicity (GRAVY) : Not available
Isoelectric point : Not available
Charge (pH 7) : Not available
Aromaticity : Not available
Molar extinction coefficient (cysteine, cystine): Not available
Hydrophobic/hydrophilic ratio : Not available
hydrophobic moment : Not available
Missing amino acid : Not available
Most occurring amino acid : Not available
Most occurring amino acid frequency : Not available
Least occurring amino acid : Not available
Least occurring amino acid frequency : Not available
Structural Information
3D-structure: Not available
Secondary structure fraction (Helix, Turn, Sheet): Not available
SMILES Notation: Not available
Secondary Structure :
| Method | Prediction |
|---|---|
| GOR | Not available |
| Chou-Fasman (CF) | Not available |
| Neural Network (NN) | Not available |
| Joint/Consensus | Not available |
Molecular Descriptors and ADMET Properties
Molecular descriptors: Not available
ADMET properties: Not available
Cross Referencing Databases databases
Pubmed Id : 24676901, .
Uniprot : Not available
CancerPPD : Click here
ApIAPDB : Not available
Reference
1 : Camilio KA, et al. Complete regression and systemic protective immune responses obtained in B16 melanomas after treatment with LTX-315. Cancer Immunol Immunother. 2014; 63:601-13. doi: 10.1007/s00262-014-1540-0
Literature
Paper title : Complete regression and systemic protective immune responses obtained in B16 melanomas after treatment with LTX-315.
Doi : https://doi.org/10.1007/s00262-014-1540-0
Abstract : Malignant melanoma is the most aggressive and deadliest form of skin cancer due to its highly metastatic potential, which calls for new and improved therapies. Cationic antimicrobial peptides (CAPs) are naturally occurring molecules found in most species, in which they play a significant role in the first line of defense against pathogens, and several CAPs have shown promising potential as novel anticancer agents. Structure-activity relationship studies on the CAP bovine lactoferricin allowed us to de novo design short chemically modified lytic anticancer peptides. In the present study, we investigated the in vivo antitumor effects of LTX-315 against intradermally established B16 melanomas in syngeneic mice. Intratumoral administration of LTX-315 resulted in tumor necrosis and the infiltration of immune cells into the tumor parenchyma followed by complete regression of the tumor in the majority of the animals. LTX-315 induced the release of danger-associated molecular pattern molecules such as the high mobility group box-1 protein in vitro and the subsequent upregulation of proinflammatory cytokines such as interleukin (IL) 1β, IL6 and IL18 in vivo. Animals cured by LTX-315 treatment were protected against a re-challenge with live B16 tumor cells both intradermally and intravenously. Together, our data indicate that intratumoral treatment with LTX-315 can provide local tumor control followed by protective immune responses and has potential as a new immunotherapeutic agent.