ROSA MARIA CHURA CHAMBI
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Artigo IPEN-doc 20281 VapC from the leptospiral VapBC toxin-antitoxin module display ribonuclease activity on the initiator tRNA2014 - LOPES, ALEXANDRE P.Y.; LOPES, LUANA M.; FRAGA, TATIANA R.; CHURA-CHAMBI, ROSA M.; SANSON, ANDRE L.; CHENG, ELISABETH; NAKAJIMA, ERIKA; MORGANTI, LIGIA; MARTINS, ELIZABETH A.L.Artigo IPEN-doc 20203 Investigation on solubilization protocols in the refolding of the thiredoxin TsnC from Xylella fastidiosa by high hydrostatic pressure approach2015 - LEMKE, LAURA S.; CHURA-CHAMBI, ROSA M.; RODRIGUES, DANIELLA; CUSSIOL, JOSE R.R.; MALAVASI, NATALIA V.; ALEGRIA, THIAGO G.P.; SOARES NETTO, LUIS E.; MORGANTI, LIGIAArtigo IPEN-doc 20095 Effect of pressure on refolding of recombinant pentameric cholera toxin B2014 - RODRIGUES, D.; FARINHA-ARCIERI, L.E.; VENTURA, A.M.; CHURA-CHAMBI, R.M.; MALAVASI, R.V.; LEMKE, L.S.; GUIMARAES, J.S.; HO, P.L.; MORGANTI, L.The production of recombinant proteins is an essential tool for the expansion of modern biological research and biotechnology. The expression of heterologous proteins in Escherichia coli often results in an incomplete folding process that leads to the accumulation of inclusion bodies (IB), aggregates that hold a certain degree of native-like secondary structure. High hydrostatic pressure (HHP) impairs intermolecular hydrophobic and electrostatic interactions, leading to dissociation of aggregates under non-denaturing conditions and is therefore a useful tool to solubilize proteins for posterior refolding. Cholera toxin (CT) is composed of a non-toxic pentamer of B subunits (CTB), a useful adjuvant in vaccines, and a toxic subunit A (CTA). We studied the process of refolding of CTB using HHP. HHP was shown to be effective for dissociation of CTB monomers from IB. Posterior incubation at atmospheric pressure of concentrated CTB (1 mg/ml) is necessary for the association of the monomers. Pentameric CTB was obtained when suspensions of CTB IB were compressed at 2.4 kbar for 16 h in the presence of Tween 20 and incubated at 1 bar for 120 h. Soluble and biologically active pentameric CTB was obtained, with a yield of 213 mg CTB/liter of culture. The experience gained in this study can be important to improve the refolding of proteins with quaternary structure.Resumo IPEN-doc 18947 Application of high hydrostatic pressure for recovery of biologically active cruzain from recombinant inclusion bodies2011 - CHAMBI, ROSA M.C.; LEMKE, LAURA S.; VALLEJO, NATALIA M.; JULIANO NETO, LUIZ; MORGANTI, LIGIAArtigo IPEN-doc 19586 The effect of temperature on protein refolding at high pressure enhanced green fluorescent protein as a model2014 - MALAVASI, N.V.; CORDEIRO, Y.; RODRIGUES, D.; CHURA-CHAMBI, R.M.; LEMKE, L.S.; MORGANTI, L.Artigo IPEN-doc 19555 Refolding of the recombinant protein Sm29, a step toward the production of the vaccine candidate against schistosomiases2013 - CHURA-CHAMBI, ROSA M.; NAKAJIMA, ERIKA; CARVALHO, ROBERTA R. de; MIYASATO, PATRICIA A.; OLIVEIRA, SÉRGIO C.; MORGANTI, LIGIA; MARTINS, ELIZABETH A.L.Artigo IPEN-doc 19227 An analysis of the factors that affect the dissociation of inclusion bodies and the refolding of endostatin under high pressure2013 - CHURA-CHAMBI, R.M.; CORDEIRO, Y.; MALAVASI, N.V.; LEMKE, L.S.; RODRIGUES, D.; MORGANTI, L.Artigo IPEN-doc 13750 Refolding of endostatin from inclusion bodies using high hydrostatic pressure2008 - CHURA-CHAMBI, ROSA M.; GENOVA, LUIS A.; AFFONSO, REGINA; MORGANTI, LIGIAArtigo IPEN-doc 15644 Refolding on the recombinant protein OmpA70 from Leptospira interrogans from inclusion bodies using high hydrostatic pressure and partial characterization of its immunological properties2010 - FRAGA, TATIANA R.; CHURA-CHAMBI, ROSA M.; GONCALEZ, AMANE P.; MORAIS, ZENAIDE M.; VASCONCELLOS, SILVIO A.; MORGANTI, LIGIA; MARTINS, ELIZABETH A.L.Artigo IPEN-doc 17408 Refolding by high pressure of a toxin containing seven disulfide bonds: bothropstoxin-1 from Bothrops jararacussu2011 - BALDUINO, KELI N.; SPENCER, PATRICK J.; MALAVASI, NATALIA V.; CHURA-CHAMBI, ROSA M.; LEMKE, LAURA S.; MORGANTI, LIGIA