dbacp03484
General Description
Peptide name : K6-Nal2-S1
Source/Organism : Not found
Linear/Cyclic : Not found
Chirality : D
Sequence Information
Sequence : Ac-KKKKKK-NAl-NAl-KKWRKWLAKK-NH2
Peptide length: Not available
C-terminal modification: Not found
N-terminal modification : Free
Non-natural peptide information: None
Activity Information
Assay type : MTT assay
Assay time : 24h
Activity : MIC : 3.1 μM
Cell line : SAS
Cancer type : Oral cancer
Other activity : Not found
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 : 25970292, .
Uniprot : Not available
CancerPPD : Not available
ApIAPDB : Not available
Reference
1 : Chu HL, et al. Novel antimicrobial peptides with high anticancer activity and selectivity. PLoS One. 2015; 10:e0126390. doi: 10.1371/journal.pone.0126390
Literature
Paper title : Novel antimicrobial peptides with high anticancer activity and selectivity.
Doi : https://doi.org/10.1371/journal.pone.0126390
Abstract : We describe a strategy to boost anticancer activity and reduce normal cell toxicity of short antimicrobial peptides by adding positive charge amino acids and non-nature bulky amino acid β-naphthylalanine residues to their termini. Among the designed peptides, K4R2-Nal2-S1 displayed better salt resistance and less toxicity to hRBCs and human fibroblast than Nal2-S1 and K6-Nal2-S1. Fluorescence microscopic studies indicated that the FITC-labeled K4R2-Nal2-S1 preferentially binds cancer cells and causes apoptotic cell death. Moreover, a significant inhibition in human lung tumor growth was observed in the xenograft mice treated with K4R2-Nal2-S1. Our strategy provides new opportunities in the development of highly effective and selective antimicrobial and anticancer peptide-based therapeutics.