Publications by authors named "Natalia V Malavasi"

Article Synopsis
  • * High hydrostatic pressure (HHP) is shown to disrupt protein aggregates, allowing for better solubilization and refolding, with TsnC serving as a model protein for the experiments.
  • * Optimal conditions for refolding were identified, achieving an 81% yield of biologically active TsnC, paving the way for future efficient HHP-based processes for other proteins.
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Aggregation is a serious obstacle for recovery of biologically active heterologous proteins from inclusion bodies (IBs) produced by recombinant bacteria. E. coli transformed with a vector containing the cDNA for Bothropstoxin-1 (BthTx-1) expressed the recombinant product as IBs.

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Background: Theracyte is a polytetrafluoroethylene membrane macroencapsulation system designed to induce neovascularization at the tissue interface, protecting the cells from host's immune rejection, thereby circumventing the problem of limited half-life and variation in circulating levels. Endostatin is a potent inhibitor of angiogenesis and tumor growth. Continuous delivery of endostatin improves the efficacy and potency of the antitumoral therapy.

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