Peptide name : L-amino acid oxidase (CC-LAAO) (LAO) (EC 1.4.3.2)

Source/Organism : Horned desert vip

Linear/Cyclic : Not found

Chirality : L

Peptide length: 516

C-terminal modification: Not found

N-terminal modification : Free

Non-natural peptide information: None

Assay type : MTT assay

Assay time : 24h

Activity : IC50 : 3.5 µg/mL

Cell line : PC12

Cancer type : Not found

Other activity : Anti-bacterial activity

Amino acid composition bar chart :

Molecular mass : 58555.8032 Dalton

Aliphatic index : 0.873

Instability index : 36.5153

Hydrophobicity (GRAVY) : -0.327

Isoelectric point : 6.0077

Charge (pH 7) : -6.43

Aromaticity : 0.110

Molar extinction coefficient (cysteine, cystine): (67730, 67980)

Hydrophobic/hydrophilic ratio : 0.92537313

hydrophobic moment : 0.103

Missing amino acid : None

Most occurring amino acid : L

Most occurring amino acid frequency : 45

Least occurring amino acid : C

Least occurring amino acid frequency : 5

Secondary structure fraction (Helix, Turn, Sheet): (0.3, 0.2, 0.3)

SMILES Notation: 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C)C)C(C)C

1 : Abdelkafi-Koubaa Z, et al. Interaction of a snake venom L-amino acid oxidase with different cell types membrane. Int J Biol Macromol. 2016; 82:757-64. doi: 10.1016/j.ijbiomac.2015.09.065

Paper title : Interaction of a snake venom L-amino acid oxidase with different cell types membrane.

Doi : https://doi.org/10.1016/j.ijbiomac.2015.09.065

Abstract : Snake venom l-amino acid oxidases are multifunctional enzymes that exhibited a wide range of pharmacological activities. Although it has been established that these activities are primarily caused by the H2O2 generated in the enzymatic reaction, the molecular mechanism, however, has not been fully investigated. In this work, LAAO interaction with cytoplasmic membranes using different cell types and Langmuir interfacial monolayers was evaluated. The Cerastes cerastes venom LAAO (CC-LAAO) did not exhibit cytotoxic activities against erythrocytes and peripheral blood mononuclear cells (PBMC). However, CC-LAAO caused cytotoxicity on several cancer cell lines and induced platelet aggregation in dose-dependent manner. Furthermore, the enzyme showed remarkable effect against Gram-positive and Gram-negative bacteria. These activities were inhibited on the addition of catalase or substrate analogs, suggesting that H2O2 liberation× is required for these effects. Binding studies revealed that CC-LAAO binds to the cell surface and enables the production of highly localized concentration of H2O2 in or near the binding interfaces. On another hand, the interaction of CC-LAAO with a mimetic phospholipid film was evaluated, for the first time, using a monomolecular film technique. Results indicated that phospholipid/CC-LAAO interactions are not involved in their binding to membrane and in their pharmacological activities.