Data/hora: 03/06/2024 16:12:32

Provedor de dados: 	80	
País: 	Brazil	
Título: 	BaltDC: purification, characterization and infrared spectroscopy of an antiplatelet DC protein isolated from Bothrops alternatus snake venom	
Autores: 	Matias,Mariana Santos; Sousa,Bruna Barbosa de; Pereira,Déborah Fernanda da Cunha; Dias,Edigar Henrique Vaz; Mamede,Carla Cristine Neves; Queiroz,Mayara Ribeiro de; Silva,Anielle Christine Almeida; Dantas,Noelio Oliveira; Soares,Andreimar Martins; Costa,Júnia de Oliveira; Oliveira,Fábio de.	
Data: 	2017-01-01	
Ano: 	2017	
Palavras-chave: 	Snake venom; Bothrops alternatus; DC protein; Platelet aggregation.	
Resumo: 	Abstract  Background: 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       PO 3  2 −  groups, present in BaltDC, form hydrogen bonds with the       PO 2 −  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.	
Tipo: 	Info:eu-repo/semantics/article	
Idioma: 	Inglês	
Identificador: 	http://www.scielo.br/scielo.php?script=sci_arttext&pid=S1678-91992017000100324	
Editor: 	Centro de Estudos de Venenos e Animais Peçonhentos	
Relação: 	10.1186/s40409-017-0126-7	
Formato: 	text/html	
Fonte: 	Journal of Venomous Animals and Toxins including Tropical Diseases  v.23 2017	
Fonte: 	info:eu-repo/semantics/openAccess