Peptide name : MP12

Source/Organism : Not found

Linear/Cyclic : Linear

Chirality : L

Peptide length: 12

C-terminal modification: Linear

N-terminal modification : Not found

Non-natural peptide information: None

Assay type : MTT assay

Assay time : Not found

Activity : IC50 : 24.7 ± 0.34 Μm

Cell line : Hep-2

Cancer type : Laryngeal cancer

Other activity : Not found

Amino acid composition bar chart :

Molecular mass : 1338.6182 Dalton

Aliphatic index : 0.891

Instability index : 38.8667

Hydrophobicity (GRAVY) : 0.3667

Isoelectric point : 5.0602

Charge (pH 7) : -1.4312

Aromaticity : 0

Molar extinction coefficient (cysteine, cystine): (0, 125)

Hydrophobic/hydrophilic ratio : 3

hydrophobic moment : -0.156

Missing amino acid : R,W,Q,T,E,K,S,F,Y,A,G

Most occurring amino acid : P

Most occurring amino acid frequency : 3

Least occurring amino acid : M

Least occurring amino acid frequency : 1

Secondary structure fraction (Helix, Turn, Sheet): (0.1, 0.4, 0.2)

SMILES Notation: CC[C@H](C)[C@H](NC(=O)[C@H](CS)NC(=O)[C@@H](NC(=O)[C@H](Cc1c[nH]cn1)NC(=O)[C@H](CC(N)=O)NC(=O)[C@H](CC(=O)O)NC(=O)[C@@H](N)CCSC)C(C)C)C(=O)N1CCC[C@H]1C(=O)N[C@@H](CC(C)C)C(=O)N[C@@H](CS)C(=O)N1CCC[C@H]1C(=O)N1CCC[C@H]1C(=O)O

1 : Velayutham M, et al. Antiproliferation of MP12 derived from a fungus, Aphanomyces invadans virulence factor, cysteine-rich trypsin inhibitor on human laryngeal epithelial cells, and in vivo zebrafish embryo model. Toxicon. 2022; 210:100-108. doi: 10.1016/j.toxicon.2022.02.019

Paper title : Antiproliferation of MP12 derived from a fungus, Aphanomyces invadans virulence factor, cysteine-rich trypsin inhibitor on human laryngeal epithelial cells, and in vivo zebrafish embryo model.

Doi : https://doi.org/10.1016/j.toxicon.2022.02.019

Abstract : Peptide-based drug development is an emerging and promising approach in cancer therapeutics. The present study focuses on understanding the mechanism of MP12 peptide (MDNHVCIPLCPP) derived from cysteine-rich trypsin inhibitor protein of virulence factor of pathogenic fungus Aphanomyces invadans. MP12 is involved in antiproliferative activity against the human laryngeal epithelial cell (Hep-2), demonstrated in this study. MP12 sequence showed a significant binding score and has multiple hydrogen bond interactions with the proteins that play a vital role in apoptotic pathways such as Bcl-2, caspase-3, caspase-7, and XIAP. Based on the bioinformatics characterization and molecular docking result, further study was focused on MP12 antiproliferative activity. The peptide showed a dose-dependent inhibition against Hep-2 cell line proliferation, analyzed over MTT and neutral red uptake assays. The IC₅₀ value of the MP12 peptide was calculated based on the antiproliferative property (24.7 ± 0.34 μM). MP12 treated Hep-2 cells showed significant shrinkage in cell morphology compared to untreated cells, inhibiting the cell cycle. The gene expression analysis validated that the MP12 significantly upregulates the caspase-3, caspase-7, and caspase-9 genes. The developmental toxicity study using zebrafish embryos as in vivo model proved that the MP12 is nontoxic. Based on the obtained results, we proposed that the peptide MP12 derived from cysteine-rich trypsin inhibitor protein of virulence molecule of pathogenic fungus have a potential antiproliferative activity. However, further clinical trials need to be focused on the mechanism and therapeutic application against laryngeal cancer.