FELIPE SENNE DE OLIVEIRA LINO
3 resultados
Resultados de Busca
Agora exibindo 1 - 3 de 3
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.Resumo IPEN-doc 22215 Construção de vetores plasmídicos para expressão de proteínas de fusão: endostatina + peptídeos com atividade pró-apoptótica2005 - LINO, FELIPE S. de O.; DIAS, LIGIA E.M.F.Resumo IPEN-doc 08440 Construção de vetores plasmídicos para expressão de proteínas de fusão: endostatina + peptídeos com atividade pró-apoptótica2004 - LINO, FELIPE S. de O.; DIAS, LIGIA E.M.F.