Please use this identifier to cite or link to this item: http://repositorio.unicamp.br/jspui/handle/REPOSIP/244424
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dc.contributor.CRUESPUNIVERSIDADE ESTADUAL DE CAMPINASpt_BR
dc.contributor.authorunicampCarregari, Victor Corasollapt_BR
dc.contributor.authorunicampPonce-Soto, Luis Albertopt_BR
dc.contributor.authorunicampMarangoni, Sérgiopt_BR
dc.typeArtigopt_BR
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 analysespt_BR
dc.contributor.authorCarregari, Victor Corasollapt_BR
dc.contributor.authorDai, Jiept_BR
dc.contributor.authorVerano-Braga, Thiagopt_BR
dc.contributor.authorRocha, Thalitapt_BR
dc.contributor.authorPonce-Soto, Luis Albertopt_BR
dc.contributor.authorMarangoni, Sergiopt_BR
dc.contributor.authorRoepstorff, Peterpt_BR
dc.subjectSequência de aminoácidospt_BR
dc.subjectBothriopsis taeniatapt_BR
dc.subjectVenenos de serpentespt_BR
dc.subjectEspectrometria de massapt_BR
dc.subjectAtividade biológicapt_BR
dc.subject.otherlanguageBothriopsis taeniatapt_BR
dc.subject.otherlanguagePhospholipase A2pt_BR
dc.subject.otherlanguageMass spectrometrypt_BR
dc.subject.otherlanguageAmino acid sequencept_BR
dc.subject.otherlanguageBiological activitypt_BR
dc.subject.otherlanguageSnake venomspt_BR
dc.description.abstractSnake 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 proteinpt_BR
dc.relation.ispartofJournal of proteomicspt_BR
dc.relation.ispartofabbreviationJ. proteomicspt_BR
dc.publisher.cityAmsterdam pt_BR
dc.publisher.countryPaíses Baixospt_BR
dc.publisherElsevierpt_BR
dc.date.issued2016pt_BR
dc.date.monthofcirculationJan.pt_BR
dc.identifier.citationRevealing 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.pt_BR
dc.language.isoengpt_BR
dc.description.volume131pt_BR
dc.description.firstpage131pt_BR
dc.description.lastpage139pt_BR
dc.rightsfechadopt_BR
dc.sourceWOSpt_BR
dc.identifier.issn1874-3919pt_BR
dc.identifier.eissn1876-7737pt_BR
dc.identifier.doi10.1016/j.jprot.2015.10.020pt_BR
dc.identifier.urlhttp://www.sciencedirect.com/science/article/pii/S1874391915301639pt_BR
dc.description.sponsorshipCONSELHO NACIONAL DE DESENVOLVIMENTO CIENTÍFICO E TECNOLÓGICO - CNPQpt_BR
dc.description.sponsorshipCOORDENAÇÃO DE APERFEIÇOAMENTO DE PESSOAL DE NÍVEL SUPERIOR - CAPESpt_BR
dc.description.sponsorship1CAPES - COORDENAÇÃO DE APERFEIÇOAMENTO DE PESSOAL DE NÍVEL SUPERIORpt_BR
dc.description.sponsorship1CNPQ - CONSELHO NACIONAL DE DESENVOLVIMENTO CIENTÍFICO E TECNOLÓGICOpt_BR
dc.description.sponsordocumentnumbersem informaçãopt_BR
dc.description.sponsordocumentnumbersem informaçãopt_BR
dc.date.available2016-06-07T13:37:08Z-
dc.date.accessioned2016-06-07T13:37:08Z-
dc.description.provenanceMade available in DSpace on 2016-06-07T13:37:08Z (GMT). No. of bitstreams: 1 wos_000366540200014.pdf: 1807755 bytes, checksum: f059e9784a6221e52457943ef8e99a8c (MD5) Previous issue date: 2016 Bitstreams deleted on 2020-06-15T14:12:12Z: wos_000366540200014.pdf,en
dc.identifier.urihttp://repositorio.unicamp.br/jspui/handle/REPOSIP/244424-
dc.contributor.departmentsem informaçãopt_BR
dc.contributor.departmentsem informaçãopt_BR
dc.contributor.departmentDepartamento de Bioquímica e Biologia Tecidualpt_BR
dc.contributor.unidadeInstituto de Biologiapt_BR
dc.subject.keywordPLA2pt_BR
dc.subject.keywordPeakspt_BR
dc.subject.keywordLTQ Orbitrap Velospt_BR
dc.subject.keywordMyotoxic activitypt_BR
dc.subject.keywordSnake venompt_BR
dc.identifier.source000366540200014-
dc.creator.orcid0000-0001-6863-1333pt_BR
dc.creator.orcid0000-0001-5976-2913pt_BR
dc.creator.orcidsem informaçãopt_BR
dc.type.formArtigo de pesquisapt_BR
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