dbACP: A Comprehensive Database of Anti-Cancer Peptides

dbacp03482

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 : C9

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.