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Type: Artigo
Title: Revealing the functional structure of a new PLA(2) K49 from Bothriopsis taeniata snake venom employing automatic "de novo" sequencing using CID/HCD/ETD MS/MS analyses
Author: Carregari, Victor Corasolla
Dai, Jie
Verano-Braga, Thiago
Rocha, Thalita
Ponce-Soto, Luis Alberto
Marangoni, Sergio
Roepstorff, Peter
Abstract: Snake venoms are composed of approximately 90% of proteins with several pharmacological activities having high potential in research as biological tools. One of the most abundant compounds is phospholipases A(2) (PLA(2)), which are the most studied venom protein due to their wide pharmacological activity. Using a combination of chromatographic steps, a new PLA(2) K49 was isolated and purified from the whole venom of the Bothriopsis taeniata and submitted to analyses mass spectrometry. An automatic "de novo" sequencing of this new PLA(2) K49 denominated Btt-TX was performed using Peaks Studio 6 for analysis of the spectra. Additionally, a triplex approach CID/HCD/ETD has been performed, to generate higher coverage of the sequence of the protein. Structural studies correlating biological activities were made associating specific Btt-TX regions and myotoxic activity. Lysine acetylation was performed to better understand the mechanism of membrane interaction, identifying the extreme importance of the highly hydrophobic amino acids L, P and F for disruption of the membrane. Our myotoxical studies show a possible membrane disruption mechanism by Creatine Kinase release without a noticeable muscle damage, that probably occurred without phospholipid hydrolyses, but with a probable penetration of the hydrophobic amino acids present in the C-terminal region of the protein
Subject: Sequência de aminoácidos
Bothriopsis taeniata
Venenos de serpentes
Espectrometria de massa
Atividade biológica
Country: Países Baixos
Editor: Elsevier
Citation: Revealing The Functional Structure Of A New Pla(2) K49 From Bothriopsis Taeniata Snake Venom Employing Automatic "de Novo" Sequencing Using Cid/hcd/etd Ms/ms Analyses. Elsevier Science Bv, v. 131, p. 131-139 Jan-2016.
Rights: fechado
Identifier DOI: 10.1016/j.jprot.2015.10.020
Date Issue: 2016
Appears in Collections:IB - Artigos e Outros Documentos

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