ROSA MARIA CHURA CHAMBI
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Artigo IPEN-doc 22822 Structural studies of the protein endostatin in fusion with BAX BH3 death domain, a hybrid that presents enhanced antitumoral activity2017 - CHURA-CHAMBI, ROSA M.; ARCURI, HELEN A.; LINO, FELIPE; VERSATI, NATAN; PALMA, MARIO S.; FAVARO, DENIZE C.; MORGANTI, LIGIAEndostatin (ES) is an antiangiogenic protein that exhibits antitumor activity in animal models. However, the activity observed in animals was not observed in human clinical trials. ES-BAX is a fusion protein composed of two functional domains: ES, which presents specificity and is internalized by activated endothelial cells and the proapoptotic BH3 domain of the protein BAX, a peptide inductor of cellular death when internalized. We have previously shown (Chura-Chambi et al., Cell Death Dis, 5, e1371, 2014) that ES-BAX presents improved antitumor activity in relation to wild-type ES. Secondary and tertiary structures of ES-BAX are similar to ES, as indicated by homology-modeling studies and molecular dynamics simulations. Tryptophan intrinsic fluorescence and circular dichroism spectroscopy corroborate these data. 15N HSQC NMR indicates that ES-BAX is structured, but some ES residues have suffered chemical shift perturbations, suggesting that the BH3 peptide interacts with some parts of the ES protein. ES and ES-BAX present similar stability to thermal denaturation. The production of stable hybrid proteins can be a new approach to the development of therapeutic agents presenting specificity for tumoral endothelium and improved antitumor effect.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, LIGIA