The role of the C-terminal region of pulchellin A-chain in the interaction with membrane model systems

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dc.contributor.authorReyes, Luis Fernando
dc.contributor.authorNobre, Thatyane Morimoto
dc.contributor.authorPavinatto, Felippe José
dc.contributor.authorZaniquelli, Maria Elisabete Darbello
dc.contributor.authorCaseli, Luciano [UNIFESP]
dc.contributor.authorOliveira, Osvaldo N.
dc.contributor.authorAraujo, Ana Paula Ulian
dc.contributor.institutionUniversidade de São Paulo (USP)
dc.contributor.institutionUniversidade Federal de São Paulo (UNIFESP)
dc.date.accessioned2016-01-24T14:17:35Z
dc.date.available2016-01-24T14:17:35Z
dc.date.issued2012-01-01
dc.description.abstractPulchellin is a Ribosome Inactivating Protein containing an A-chain (PAC), whose toxic activity requires crossing the endoplasmic reticulum (ER) membrane. in this paper, we investigate the interaction between recombinant PAC (rPAC) and Langmuir monolayers of dipalmitoyl phosphatidyl glycerol (DPPG), which served as membrane model. Three catalytically active, truncated PACs with increasing deletion of the C-terminal region, possessing 244,239 and 236 residues (rPAC(244), rPAC(239) and rPAC(236)), were studied. rPAC had the strongest interaction with the DPPG monolayer, inducing a large expansion in its surface pressure-area isotherm. the affinity to DPPG decreased with increased deletion of the C-terminal region. When the C-terminal region was deleted completely (rPAC(236)), the interaction was recovered, probably because other hydrophobic regions were exposed to the membrane. Using Polarization Modulated-Infrared Reflection Absorption Spectroscopy (PM-IRRAS) we observed that at a bare air/water interface rPAC comprised mainly alpha-helix structures, the C-terminal region had unordered structures when interacting with DPPG. for rPAC(236) the alpha-helices were preserved even in the presence of DPPG. These results confirm the importance of the C-terminal region for PAC-ER membrane interaction. the partial unfolding only with preserved C-terminal appears a key step for the protein to reach the cytosol and develop its toxic activity. (C) 2011 Elsevier B.V. All rights reserved.en
dc.description.affiliationUniv São Paulo, Inst Fis Sao Carlos, Ctr Biotecnol Mol Estrut, BR-13560970 Sao Carlos, SP, Brazil
dc.description.affiliationUniv São Paulo, Inst Fis Sao Carlos, Grp Polimeros Bernhard Gross, BR-13560970 Sao Carlos, SP, Brazil
dc.description.affiliationUniv São Paulo, Fac Filosofia Ciencias & Letras Ribeirao Preto, Dept Quim, BR-14049 Ribeirao Preto, SP, Brazil
dc.description.affiliationUniversidade Federal de São Paulo, Inst Ciencias Ambientais Quim & Farmaceut, Diadema, SP, Brazil
dc.description.affiliationUnifespUniversidade Federal de São Paulo, Inst Ciencias Ambientais Quim & Farmaceut, Diadema, SP, Brazil
dc.description.sourceWeb of Science
dc.description.sponsorshipFundação de Amparo à Pesquisa do Estado de São Paulo (FAPESP)
dc.description.sponsorshipConselho Nacional de Desenvolvimento Científico e Tecnológico (CNPq)
dc.format.extent82-89
dc.identifierhttp://dx.doi.org/10.1016/j.bbamem.2011.10.002
dc.identifier.citationBiochimica Et Biophysica Acta-biomembranes. Amsterdam: Elsevier B.V., v. 1818, n. 1, p. 82-89, 2012.
dc.identifier.doi10.1016/j.bbamem.2011.10.002
dc.identifier.fileWOS000298461100011.pdf
dc.identifier.issn0005-2736
dc.identifier.urihttp://repositorio.unifesp.br/handle/11600/34337
dc.identifier.wosWOS:000298461100011
dc.language.isoeng
dc.publisherElsevier B.V.
dc.relation.ispartofBiochimica Et Biophysica Acta-biomembranes
dc.rightsinfo:eu-repo/semantics/openAccess
dc.rights.licensehttp://www.elsevier.com/about/open-access/open-access-policies/article-posting-policy
dc.subjectRibosome inactivating proteinen
dc.subjectLangmuir monolayersen
dc.subjectPulchellinen
dc.subjectMembrane interactionen
dc.subjectPM-IRRASen
dc.titleThe role of the C-terminal region of pulchellin A-chain in the interaction with membrane model systemsen
dc.typeinfo:eu-repo/semantics/article
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