Baltetin: a new C-type lectin-like isolated from Bothrops alternatus snake venom which act as a platelet aggregation inhibiting

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dc.contributor.authorPereira, Déborah Fernanda da Cunha
dc.contributor.authorMatias Ribeiro, Mariana Santos
dc.contributor.authorde Sousa Simamoto, Bruna Barbosa
dc.contributor.authorDias, Edigar Henrique Vaz
dc.contributor.authorCosta, Júnia de Oliveira
dc.contributor.authorSantos-Filho, Norival Alves [UNESP]
dc.contributor.authorBordon, Karla de Castro Figueiredo
dc.contributor.authorArantes, Eliane Candiani
dc.contributor.authorDantas, Noelio Oliveira
dc.contributor.authorSilva, Anielle Christine Almeida
dc.contributor.authorde Oliveira, Fábio
dc.contributor.authorMamede, Carla Cristine Neves
dc.contributor.institutionUniversidade Federal de Uberlândia (UFU)
dc.contributor.institutionUnidade Ituiutaba
dc.contributor.institutionCiência e Tecnologia do Triângulo Mineiro
dc.contributor.institutionUniversidade Estadual Paulista (Unesp)
dc.contributor.institutionUniversidade de São Paulo (USP)
dc.contributor.institutionUniversidade Federal de Alagoas
dc.date.accessioned2021-06-25T10:59:52Z
dc.date.available2021-06-25T10:59:52Z
dc.date.issued2021-05-30
dc.description.abstractC-type lectin-like proteins found in snake venom, known as snaclecs, have important effects on hemostasis through targeting membrane receptors, coagulation factors and other hemostatic proteins. Here, we present the isolation and functional characterization of a snaclec isolated from Bothrops alternatus venom, designated as Baltetin. We purified the protein in three chromatographic steps (anion-exchange, affinity and reversed-phase chromatography). Baltetin is a dimeric snaclec that is approximately 15 and 25 kDa under reducing and non-reducing conditions, respectively, as estimated by SDS-PAGE. Matrix-assisted laser desorption and ionization time-of-flight mass spectrometry and Edman degradation sequencing revealed that Baltetin is a heterodimer. The first 40 amino acid residues of the N-terminal region of Baltetin subunits share a high degree of sequence identity with other snaclecs. Baltetin had a specific, dose-dependent inhibitory effect on epinephrine-induced platelet aggregation in human platelet-rich plasma, inhibiting up to 69% of platelet aggregation. Analysis of the infrared spectra suggested that the interaction between Baltetin and platelets can be attributed to the formation of hydrogen bonds between the PO32- groups in the protein and PO2- groups in the platelet membrane. This interaction may lead to membrane lipid peroxidation, which prevents epinephrine from binding to its receptor. The present work suggests that Baltetin, a new C-type lectin-like protein isolated from B. alternatus venom, is the first snaclec to inhibit epinephrine-induced platelet aggregation. This could be of medical interest as a new tool for the development of novel therapeutic agents for the prevention and treatment of thrombotic disorders.en
dc.description.affiliationInstituto de Biotecnologia Universidade Federal de Uberlândia, Campus Uberlândia
dc.description.affiliationInstituto de Ciências Biomédicas Universidade Federal de Uberlândia, Campus Uberlândia
dc.description.affiliationUniversidade do Estado de Minas Gerais Unidade Ituiutaba
dc.description.affiliationInstituto Federal de Educação Ciência e Tecnologia do Triângulo Mineiro, Campus Ituiutaba
dc.description.affiliationUNESP - Universidade Estadual Paulista, Campus Experimental de Registro
dc.description.affiliationFaculdade de Ciências Farmacêuticas de Ribeirão Preto Universidade de São Paulo
dc.description.affiliationInstituto de Física Universidade Federal de Alagoas
dc.description.affiliationUnespUNESP - Universidade Estadual Paulista, Campus Experimental de Registro
dc.identifierhttp://dx.doi.org/10.1016/j.jchromb.2021.122695
dc.identifier.citationJournal of Chromatography B: Analytical Technologies in the Biomedical and Life Sciences, v. 1173.
dc.identifier.doi10.1016/j.jchromb.2021.122695
dc.identifier.issn1873-376X
dc.identifier.issn1570-0232
dc.identifier.scopus2-s2.0-85105691170
dc.identifier.urihttp://hdl.handle.net/11449/207721
dc.language.isoeng
dc.relation.ispartofJournal of Chromatography B: Analytical Technologies in the Biomedical and Life Sciences
dc.sourceScopus
dc.subjectBothrops alternatus
dc.subjectPlatelet aggregation
dc.subjectSnaclecs
dc.subjectSnake venom
dc.titleBaltetin: a new C-type lectin-like isolated from Bothrops alternatus snake venom which act as a platelet aggregation inhibitingen
dc.typeArtigo
unesp.departmentEngenharia Agronômica - FCAVRpt

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Registro - FCAVR - Faculdade de Ciências Agrárias do Vale do Ribeira