Please use this identifier to cite or link to this item: https://www.arca.fiocruz.br/handle/icict/32711
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dc.contributor.authorMatias, Mariana Santos
dc.contributor.authorSousa, Bruna Barbosa de
dc.contributor.authorPereira, Déborah Fernanda da Cunha
dc.contributor.authorDias, Edigar Henrique Vaz
dc.contributor.authorMamede, Carla Cristine Neves
dc.contributor.authorQueiroz, Mayara Ribeiro de
dc.contributor.authorSilva, Anielle Christine Almeida
dc.contributor.authorDantas, Noelio Oliveira
dc.contributor.authorSoares, Andreimar Martins
dc.contributor.authorCosta, Júnia de Oliveira
dc.contributor.authorOliveira, Fábio de
dc.date.accessioned2019-04-24T14:06:22Z
dc.date.available2019-04-24T14:06:22Z
dc.date.issued2017
dc.identifier.citationMATIAS, M.S. et al. BaltDC: purification, characterization and infrared spectroscopy of an antiplatelet DC protein isolated from Bothrops alternatus snake venom. Journal of Venomous Animals and Toxins including Tropical Diseases, p. 1-8, 2017.
dc.identifier.issn1678-9199
dc.identifier.urihttps://www.arca.fiocruz.br/handle/icict/32711
dc.language.isoeng
dc.publisherJournal of Venomous Animals and Toxins including Tropical Diseases
dc.rightsopen access
dc.titleBaltDC: purification, characterization and infrared spectroscopy of an antiplatelet DC protein isolated from Bothrops alternatus snake venom.
dc.typeArticle
dc.identifier.doi10.1186/s40409-017-0126-7
dc.description.abstractenBackground: Snake venoms are a complex mixture of proteins, organic and inorganic compounds. Some of these proteins, enzymatic or non-enzymatic ones, are able to interact with platelet receptors, causing hemostatic disorders. The possible therapeutic potential of toxins with antiplatelet properties may arouse interest in the pharmacological areas. The present study aimed to purify and characterize an antiplatelet DC protein from Bothrops alternatus snake venom. Methods: The protein, called BaltDC (DC protein from B. alternatus snake venom), was purified by a combination of ion-exchange chromatography on DEAE-Sephacel column and gel filtration on Sephadex G-75. The molecular mass was estimated by polyacrylamide gel electrophoresis in the presence of sodium dodecyl sulfate (SDS-PAGE). The amino acid sequence of the N-terminal region was carried out by Edman degradation method. Platelet aggregation assays were performed in human platelet-rich plasma (PRP). Infrared (IR) spectroscopy was used in order to elucidate the interactions between BaltDC and platelet membrane. Results: BaltDC ran as a single protein band on SDS-PAGE and showed apparent molecular mass of 32 kDa under reducing or non-reducing conditions. The N-terminal region of the purified protein revealed the amino acid sequence IISPPVCGNELLEVGEECDCGTPENCQNECCDA, which showed identity with other snake venom metalloproteinases (SVMPs). BaltDC was devoid of proteolytic, hemorrhagic, defibrinating or coagulant activities, but it showed a specific inhibitory effect on platelet aggregation induced by ristocetin and epinephrine in PRP. IR analysis spectra strongly suggests that PO3 2− groups, present in BaltDC, form hydrogen bonds with the PO2 − groups present in the non-lipid portion of the membrane platelets. Conclusions: BaltDC may be of medical interest since it was able to inhibit platelet aggregation.
dc.creator.affilliationFederal University of Uberlândia. Institute of Genetics and Biochemistry. Postgraduate Program in Genetics and Biochemistry. Uberlândia, MG, Brasil.
dc.creator.affilliationFederal University of Uberlândia. Institute of Genetics and Biochemistry. Postgraduate Program in Genetics and Biochemistry. Uberlândia, MG, Brasil / National Institute of Science and Technology in Nanobiopharmaceutics. Belo Horizonte, MG, Brasil.
dc.creator.affilliationFederal University of Uberlândia. Institute of Genetics and Biochemistry. Postgraduate Program in Genetics and Biochemistry. Uberlândia, MG, Brasil.
dc.creator.affilliationFederal University of Uberlândia. Institute of Genetics and Biochemistry. Postgraduate Program in Genetics and Biochemistry. Uberlândia, MG, Brasil.
dc.creator.affilliationFederal University of Uberlândia. Institute of Agricultural Sciences. Monte Carmelo, MG, Brasil / National Institute of Science and Technology in Nanobiopharmaceutics. Belo Horizonte, MG, Brasil.
dc.creator.affilliationNational Institute of Science and Technology in Nanobiopharmaceutics. Belo Horizonte, MG, Brasil.
dc.creator.affilliationFederal University of Uberlândia. Institute of Physics. Uberlândia, MG, Brasil.
dc.creator.affilliationFederal University of Uberlândia. Institute of Physics. Uberlândia, MG, Brasil.
dc.creator.affilliationFundação Oswaldo Cruz. Fiocruz Rondônia. Porto Velho, RO, Brasil / Federal University of Rondônia. Center for the Study of Biomolecules Applied to Health. Porto Velho, RO, Brasil / University Center São Lucas. Porto Velho, RO, Brasil.
dc.creator.affilliationFederal University of Uberlândia. Institute of Genetics and Biochemistry. Postgraduate Program in Genetics and Biochemistry. Uberlândia, MG, Brasil / Federal Institute of Education, Science and Technology of Triângulo Mineiro. Ituiutaba, MG, Brasil.
dc.creator.affilliationFederal University of Uberlândia. Institute of Biomedical Sciences. Uberlândia, MG, Brasil / National Institute of Science and Technology in Nanobiopharmaceutics. Belo Horizonte, MG, Brasil.
dc.subject.enSnake venom
dc.subject.enBothrops alternatus
dc.subject.enDC protein
dc.subject.enPlatelet aggregation
dc.identifier.eissn1678-9199
Appears in Collections:RO - Artigos de Periódicos




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