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

dc.creatorCarregari
dc.creatorVictor Corasolla; Dai
dc.creatorJie; Verano-Braga
dc.creatorThiago; Rocha
dc.creatorThalita; Ponce-Soto
dc.creatorLuis Alberto; Marangoni
dc.creatorSergio; Roepstorff
dc.creatorPeter
dc.date2016-Jan
dc.date2016-06-07T13:37:08Z
dc.date2016-06-07T13:37:08Z
dc.date.accessioned2018-03-29T01:52:18Z
dc.date.available2018-03-29T01:52:18Z
dc.identifier
dc.identifierRevealing 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.
dc.identifier1874-3919
dc.identifierWOS:000366540200014
dc.identifier10.1016/j.jprot.2015.10.020
dc.identifierhttp://www.sciencedirect.com/science/article/pii/S1874391915301639
dc.identifierhttp://repositorio.unicamp.br/jspui/handle/REPOSIP/244424
dc.identifier.urihttp://repositorioslatinoamericanos.uchile.cl/handle/2250/1308122
dc.descriptionCoordenação de Aperfeiçoamento de Pessoal de Nível Superior (CAPES)
dc.descriptionConselho Nacional de Desenvolvimento Científico e Tecnológico (CNPq)
dc.descriptionSnake 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. (C) 2015 Elsevier B.V. All rights reserved.
dc.description131
dc.description
dc.description
dc.description131
dc.description139
dc.descriptionCoordenação de Aperfeiçoamento de Pessoal de Nível Superior (CAPES)
dc.descriptionConselho Nacional de Desenvolvimento Científico e Tecnológico (CNPq)
dc.descriptionCoordenação de Aperfeiçoamento de Pessoal de Nível Superior (CAPES)
dc.descriptionConselho Nacional de Desenvolvimento Científico e Tecnológico (CNPq)
dc.description
dc.description
dc.description
dc.languageen
dc.publisherELSEVIER SCIENCE BV
dc.publisher
dc.publisherAMSTERDAM
dc.relationJOURNAL OF PROTEOMICS
dc.rightsembargo
dc.sourceWOS
dc.subjectTandem Mass-spectrometry
dc.subjectPhospholipase A(2)
dc.subjectTityus-serrulatus
dc.subjectPeptide Identification
dc.subjectMolecular-mechanism
dc.subjectCrystal-structures
dc.subjectMoving Pieces
dc.subjectSpectra
dc.subjectToxins
dc.subjectMuscle
dc.titleRevealing 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
dc.typeArtículos de revistas


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