dbACP: A Comprehensive Database of Anti-Cancer Peptides

dbacp05584

General Description

Peptide name : Pleurocidin-a

Source/Organism : Winter flounder

Linear/Cyclic : Not found

Chirality : Not found

Sequence Information

Sequence : GWGSFFKKAAHVGKHVGKAALTHYL-NH6

Peptide length: Not available

C-terminal modification: Not found

N-terminal modification : Amidation

Non-natural peptide information: None

Activity Information

Assay type : MTT assay

Assay time : 48h

Activity : IC50 : 29.8 µM

Cell line : AGS

Cancer type : Stomach adenocarcinoma

Other activity : Anti-bacterial 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 : 36005521, .

Uniprot : Not available

CancerPPD : Not available

ApIAPDB : Not available

Reference

1 : Hsu HC, et al. Antibacterial and Anticancer Activities of Pleurocidin-Amide, a Potent Marine Antimicrobial Peptide Derived from Winter Flounder, Pleuronectes americanus. Mar Drugs. 2022; 20:(unknown pages). doi: 10.3390/md20080519

Literature

Paper title : Antibacterial and Anticancer Activities of Pleurocidin-Amide, a Potent Marine Antimicrobial Peptide Derived from Winter Flounder, Pleuronectes americanus.

Doi : https://doi.org/10.3390/md20080519

Abstract : The extensive use of conventional antibiotics has led to the growing emergence of many resistant strains of pathogenic bacteria. Evidence suggests that cationic antimicrobial peptides (AMPs) have the greatest potential to serve as traditional antibiotic substitutes. Recent studies have also reported that certain AMPs have selective toxicity toward various types of cancer cells. The electrostatic attraction between the negatively charged membrane components and AMPs is believed to play a crucial role in the disruption of bacterial and cancer cell membranes. In the current study, we used a potent AMP called Pleurocidin (Ple) derived from winter flounder Pleuronectes americanus and its C-terminal-amidated derivative Pleurocidin-amide (Ple-a), and evaluated their antibacterial and anticancer activities. Our results indicated that both Ple and Ple-a exhibited significant antibacterial activity against a broad spectrum of Gram-positive and Gram-negative bacteria, especially marine pathogens, with MIC values ranging from 0.25 to 32 μg/mL. These peptides are also potent against several multidrug-resistant (MDR) bacterial strains, with MIC values ranging from 2 to 256 μg/mL. When used in combination with certain antibiotics, they exhibited a synergistic effect against MDR E. coli. Ple and Ple-a also showed notable cytotoxicity toward various cancer cell lines, with IC<sub>50</sub> values ranging from 11 to 340 μM, while normal mouse fibroblast 3T3 cells were less susceptible to these peptides. Ple-a was then selected to study its anticancer mechanism toward A549 human lung adenocarcinoma cells. Western blot analysis and confocal microscopy showed that Ple-a could inhibit autophagy of A549 cells, and induce apoptosis 48 h after treatment. Our findings provided support for the future application of Ple-a as potential therapeutic agent for bacterial infections and cancer treatment.