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BioMed Research International
Volume 2017, Article ID 4315832, 9 pages
Research Article

A New Platelet-Aggregation-Inhibiting Factor Isolated from Bothrops moojeni Snake Venom

1Instituto de Genética e Bioquímica, Universidade Federal de Uberlândia, Uberlândia, MG, Brazil
2Instituto Nacional de Ciência e Tecnologia em Nano-Biofarmacêutica (N-Biofar), Belo Horizonte, MG, Brazil
3Instituto de Ciências Agrárias, Universidade Federal de Uberlândia, Monte Carmelo, MG, Brazil
4Instituto de Física, Universidade Federal de Uberlândia, Uberlândia, MG, Brazil
5Instituto Federal de Educação, Ciência e Tecnologia do Triângulo Mineiro, Campus Ituiutaba, Ituiutaba, MG, Brazil
6Instituto de Ciências Biomédicas, Universidade Federal de Uberlândia, Uberlândia, MG, Brazil

Correspondence should be addressed to Júnia de Oliveira Costa; rb.ude.mtfi@atsocainuj and Fábio de Oliveira; rb.ufu.amaraumu@arievilof

Received 7 July 2017; Revised 12 September 2017; Accepted 24 September 2017; Published 1 November 2017

Academic Editor: Ji-Fu Wei

Copyright © 2017 Bruna Barbosa de Sousa et al. This is an open access article distributed under the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.


This work reports the purification and functional characterization of BmooPAi, a platelet-aggregation-inhibiting factor from Bothrops moojeni snake venom. The toxin was purified by a combination of three chromatographic steps (ion-exchange on DEAE-Sephacel, molecular exclusion on Sephadex G-75, and affinity chromatography on HiTrap™ Heparin HP). BmooPAi was found to be a single-chain protein with an apparent molecular mass of 32 kDa on 14% SDS-PAGE, under reducing conditions. Sequencing of BmooPAi by Edman degradation revealed the amino acid sequence LGPDIVPPNELLEVM. The toxin was devoid of proteolytic, haemorrhagic, defibrinating, or coagulant activities and induced no significant oedema or hyperalgesia. BmooPAi showed a rather specific inhibitory effect on ristocetin-induced platelet aggregation in human platelet-rich plasma, whereas it had little or no effect on platelet aggregation induced by collagen and adenosine diphosphate. The results presented in this work suggest that BmooPAi is a toxin comprised of disintegrin-like and cysteine-rich domains, originating from autolysis/proteolysis of PIII SVMPs from B. moojeni snake venom. This toxin may be of medical interest because it is a platelet aggregation inhibitor, which could potentially be developed as a novel therapeutic agent to prevent and/or treat patients with thrombotic disorders.