Data/hora: 13/06/2024 03:37:07

Provedor de dados: 	80	
País: 	Brazil	
Título: 	Crotalus durissus terrificus crotapotin naturally displays preferred positions for amino acid substitutions	
Autores: 	Oliveira,Laudicéia Alves de; Ferreira Jr,Rui Seabra; Barraviera,Benedito; Carvalho,Francilene Capel Tavares de; Barros,Luciana Curtolo de; Santos,Lucilene Delazari dos; Pimenta,Daniel Carvalho.	
Data: 	2017-01-01	
Ano: 	2017	
Palavras-chave: 	Crotalus durissus terrificus; Venom; Crotoxin; Crotapotin; Isoforms.	
Resumo: 	Abstract  Background  Classically, Crotalus durissus terrificus (Cdt) venom can be described, according to chromatographic criteria, as a simple venom, composed of four major toxins, namely: gyroxin, crotamine, crotoxin and convulxin. Crotoxin is a non-covalent heterodimeric neurotoxin constituted of two subunits: an active phospholipase A2 and a chaperone protein, termed crotapotin. This molecule is composed of three peptide chains connected by seven disulfide bridges. Naturally occurring variants/isoforms of either crotoxin or crotapotin itself have already been reported.  Methods  The crude Cdt venom was separated by using RP-HPLC and the toxins were identified by mass spectrometry (MS). Crotapotin was purified, reduced and alkylated in order to separate the peptide chains that were further analyzed by mass spectrometry and de novo peptide sequencing.  Results  The RP-HPLC profile of the isolated crotapotin chains already indicated that the α chain would present isoforms, which was corroborated by the MS and tandem mass spectrometry analyses.  Conclusion  It was possible to observe that the Cdt crotapotin displays a preferred amino acid substitution pattern present in the α chain, at positions 31 and 40. Moreover, substitutions could also be observed in β and γ chains (one for each). The combinations of these four different peptides, with the already described chains, would produce ten different crotapotins, which is compatible to our previous observations for the Cdt venom.	
Tipo: 	Info:eu-repo/semantics/article	
Idioma: 	Inglês	
Identificador: 	http://www.scielo.br/scielo.php?script=sci_arttext&pid=S1678-91992017000100319	
Editor: 	Centro de Estudos de Venenos e Animais Peçonhentos	
Relação: 	10.1186/s40409-017-0136-5	
Formato: 	text/html	
Fonte: 	Journal of Venomous Animals and Toxins including Tropical Diseases  v.23 2017	
Fonte: 	info:eu-repo/semantics/openAccess