Peptide name : BmPLA2

Source/Organism : phospholipase A2 isoform from B. moojeni venom

Linear/Cyclic : Linear

Chirality : L

Peptide length: 24

C-terminal modification: Linear

N-terminal modification : Free

Non-natural peptide information:

Assay type : MTT assay

Assay time : 24-h

Activity : IC50 = 0.6 µM

Cell line : CaCo-2

Cancer type : Colorectal Cancer

Other activity : Anticancer

Amino acid composition bar chart :

Molecular mass : 2984.5527 Dalton

Aliphatic index : 0.529

Instability index : 18.2504

Hydrophobicity (GRAVY) : 0.2417

Isoelectric point : 9.4046

Charge (pH 7) : 1.7579

Aromaticity : 29.16

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

Hydrophobic/hydrophilic ratio : 1.1818

hydrophobic moment : 0.6713

Missing amino acid : C,D,H,N,P,R,V

Most occurring amino acid : F

Most occurring amino acid frequency : 4

Least occurring amino acid : W

Least occurring amino acid frequency : 1

Secondary structure fraction (Helix, Turn, Sheet): (37., 16., 45.)

SMILES Notation: CC[C@H](C)[C@H](NC(=O)[C@H](CCCCN)NC(=O)[C@H](CCSC)NC(=O)[C@@H](NC(=O)[C@H](CC(C)C)NC(=O)[C@H](CCSC)NC(=O)[C@H](CCC(=O)O)NC(=O)[C@H](Cc1ccccc1)NC(=O)[C@H](CCC(N)=O)NC(=O)[C@H](Cc1c[nH]c2ccccc12)NC(=O)[C@H](CCCCN)NC(=O)[C@@H](N)Cc1ccccc1)[C@@H](C)CC)C(=O)N[C@@H](C)C(=O)N[C@@H](CCCCN)C(=O)N[C@H](C(=O)N[C@@H](CO)C(=O)NCC(=O)N[C@@H](Cc1ccccc1)C(=O)N[C@@H](CCSC)C(=O)N[C@@H](Cc1ccccc1)C(=O)N[C@@H](Cc1ccc(O)cc1)C(=O)N[C@@H](CO)C(=O)N[C@@H](CO)C(=O)N[C@@H](Cc1ccc(O)cc1)C(=O)O)[C@@H](C)O

1 : Frihling BEF, et al. Purification, Characterization and Evaluation of the Antitumoral Activity of a Phospholipase A2 from the Snake Bothrops moojeni. Pharmaceuticals (Basel). 2022; 15:(unknown pages). doi: 10.3390/ph15060724

Paper title : Purification, Characterization and Evaluation of the Antitumoral Activity of a Phospholipase A2 from the Snake Bothrops moojeni.

Doi : https://doi.org/10.3390/ph15060724

Abstract : Nature presents a wide range of biomolecules with pharmacological potential, including venomous animal proteins. Among the protein components from snake venoms, phospholipases (PLA₂) are of great importance for the development of new anticancer compounds. Thus, we aimed to evaluate the PLA₂ anticancer properties from Bothrops moojeni venom. The crude venom was purified through three chromatographic steps, monitored by enzymatic activity and SDS-PAGE (12%). The purified PLA₂ denominated BmPLA2 had its molecular mass and N-terminal sequence identified by mass spectrometry and Edman degradation, respectively. BmPLA2 was assayed against human epithelial colorectal adenocarcinoma cells (Caco-2), human rhabdomyosarcoma cells (RD) and mucoepidermoid carcinoma of the lung (NCI-H292), using human fibroblast cells (MRC-5) and microglia cells (BV-2) as a cytotoxicity control. BmPLA2 presented 13,836 Da and a 24 amino acid-residue homologue with snake PLA₂, which showed a 90% similarity with other Bothrops moojeni PLA₂. BmPLA2 displayed an IC₅₀ of 0.6 µM against Caco-2, and demonstrated a selectivity index of 1.85 (compared to MRC-5) and 6.33 (compared to BV-2), supporting its selectivity for cancer cells. In conclusion, we describe a new acidic phospholipase, which showed antitumor activity and is a potential candidate in the development of new biotechnological tools.