Purification and Characterization of BmooAi: A New Toxin fromBothrops moojeniSnake Venom That Inhibits Platelet Aggregation | Zendy

Mayara Ribeiro de Queiroz | Zendy; Carla Cristine Neves Mamede | Zendy; Nadia Cristina Gomes de Morais | Zendy; Kelly Cortes Fonseca | Zendy; Bruna Barbosa de Sousa | Zendy; Thaís M. Migliorini | Zendy; Déborah Fernanda C. Pereira | Zendy; Leonilda Stanziola | Zendy; Leonardo A. Calderón | Zendy; Rodrigo SimõesSilva | Zendy; Andreimar M. Soares | Zendy; Fábio de Oliveira | Zendy

Open Access

Purification and Characterization of BmooAi: A New Toxin fromBothrops moojeniSnake Venom That Inhibits Platelet Aggregation

Author(s) -

Mayara Ribeiro de Queiroz,

Carla Cristine Neves Mamede,

Nadia Cristina Gomes de Morais,

Kelly Cortes Fonseca,

Bruna Barbosa de Sousa,

Thaís M. Migliorini,

Déborah Fernanda C. Pereira,

Leonilda Stanziola,

Leonardo A. Calderón,

Rodrigo SimõesSilva,

Andreimar M. Soares,

Fábio de Oliveira

Publication year - 2014

Publication title -

biomed research international

Language(s) - English

Resource type - Journals

SCImago Journal Rank - 0.772

H-Index - 126

eISSN - 2314-6141

pISSN - 2314-6133

DOI - 10.1155/2014/920942

Subject(s) - edman degradation , venom , chemistry , size exclusion chromatography , bothrops , snake venom , molecular mass , adenosine diphosphate , sephadex , platelet , chromatography , toxin , biochemistry , platelet aggregation inhibitor , platelet aggregation , peptide sequence , biology , enzyme , immunology , aspirin , gene

In this paper, we describe the purification/characterization of BmooAi, a new toxin from Bothrops moojeni that inhibits platelet aggregation. The purification of BmooAi was carried out through three chromatographic steps (ion-exchange on a DEAE-Sephacel column, molecular exclusion on a Sephadex G-75 column, and reverse-phase HPLC chromatography on a C2/C18 column). BmooAi was homogeneous by SDS-PAGE and shown to be a single-chain protein of 15,000 Da. BmooAi was analysed by MALDI-TOF Spectrometry and revealed two major components with molecular masses 7824.4 and 7409.2 as well as a trace of protein with a molecular mass of 15,237.4 Da. Sequencing of BmooAi by Edman degradation showed two amino acid sequences: IRDFDPLTNAPENTA and ETEEGAEEGTQ, which revealed no homology to any known toxin from snake venom. BmooAi showed a rather specific inhibitory effect on platelet aggregation induced by collagen, adenosine diphosphate, or epinephrine in human platelet-rich plasma in a dose-dependent manner, whereas it had little or no effect on platelet aggregation induced by ristocetin. The effect on platelet aggregation induced by BmooAi remained active even when heated to 100°C. BmooAi could be of medical interest as a new tool for the development of novel therapeutic agents for the prevention and treatment of thrombotic disorders.

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