Conformational changes of Loxosceles venom sphingomyelinases monitored by circular dichroism

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dc.contributor.authorAndrade, S. A. de
dc.contributor.authorPedrosa, MFF
dc.contributor.authorAndrade, RMG de
dc.contributor.authorOliva, MLV
dc.contributor.authorvan den Berge, C. W.
dc.contributor.authorTambourgi, D. V.
dc.contributor.institutionInst Butantan
dc.contributor.institutionUniversidade Federal de São Paulo (UNIFESP)
dc.contributor.institutionCardiff Univ
dc.date.accessioned2016-01-24T12:37:40Z
dc.date.available2016-01-24T12:37:40Z
dc.date.issued2005-02-04
dc.description.abstractEnvenomation by arachnids of the genus Loxosceles can induce a variety of biological effects, including dermonecrosis and hemolysis. We have previously identified in L. intermedia venom two highly homologous proteins with sphingomyelinase activity, termed P1 and P2, responsible for all these pathological events, and also an inactive isoform P3. the toxins P1 and P2 displayed 85% identity with each other at the amino acid level and showed a 57% identity with SMase I, an active toxin from L. laeta venom. Circular dichroism was used to determine and compare the solution structure of the active and inactive isoforms. Effects of pH and temperature change on the CD spectra of the toxins were investigated and correlated with the biological activities. This study sheds new light on the structure-function relationship of homologous proteins with distinct biological properties and represents the first report on the structure-function relationship of Loxosceles sphingomyelinases D. (C) 2004 Elsevier Inc. All rights reserved.en
dc.description.affiliationInst Butantan, Lab Imunoquim, São Paulo, Brazil
dc.description.affiliationUniversidade Federal de São Paulo, Lab Bioquim, São Paulo, Brazil
dc.description.affiliationCardiff Univ, Wales Coll Med, Dept Pharmacol Toxicol & Therapeut, Cardiff, S Glam, Wales
dc.description.affiliationUnifespUniversidade Federal de São Paulo, Lab Bioquim, São Paulo, Brazil
dc.description.sourceWeb of Science
dc.format.extent117-123
dc.identifierhttp://dx.doi.org/10.1016/j.bbrc.2004.11.146
dc.identifier.citationBiochemical and Biophysical Research Communications. San Diego: Academic Press Inc Elsevier Science, v. 327, n. 1, p. 117-123, 2005.
dc.identifier.doi10.1016/j.bbrc.2004.11.146
dc.identifier.issn0006-291X
dc.identifier.urihttp://repositorio.unifesp.br/handle/11600/28153
dc.identifier.wosWOS:000226345400019
dc.language.isoeng
dc.publisherElsevier B.V.
dc.relation.ispartofBiochemical and Biophysical Research Communications
dc.rightsinfo:eu-repo/semantics/restrictedAccess
dc.rights.licensehttp://www.elsevier.com/about/open-access/open-access-policies/article-posting-policy
dc.subjectLoxoscelesen
dc.subjectvenomsen
dc.subjectcircular dichroismen
dc.subjectsphingomyelinase Den
dc.subjecthemolysisen
dc.subjectdermonecrosisen
dc.titleConformational changes of Loxosceles venom sphingomyelinases monitored by circular dichroismen
dc.typeinfo:eu-repo/semantics/article
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