Person: Bianco, Valentino
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First Name
Valentino
Last Name
Bianco
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Universidad Complutense de Madrid
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Item How the stability of a folded protein depends on interfacial water properties and residue-residue interactions(Journal of molecular liquids, 2017) Bianco, Valentino; Pagès-Gelabert, Neus; Coluzza, Ivan; Franzese, GiancarloProteins tend to adopt a single or a reduced ensemble of configurations at natural conditions [1], but changes in temperature T and pressure P induce their unfolding. Therefore for each protein there is a stability region (SR) in the T–P thermodynamic plane outside which the biomolecule is denaturated. It is known that the extension and shape of the SR depend on i) the specific protein residue-residue interactions in the native state of the amino acids sequence and ii) the water properties at the hydration interface. Here we analyze by Monte Carlo simulations the different coarse-grained protein models in explicit water how changes in i) and ii) affect the SR. We show that the solvent properties ii) are essential to rationalize the SR shape at low T and high P and that our findings are robust with respect to parameter changes and with respect to different protein models, representative of the ordered and disordered proteins. These results can help in developing new strategies for the design of novel synthetic biopolymers.Item Proteins Are Solitary! Pathways of Protein Folding and Aggregation in Protein Mixtures(The Journal of Physical Chemistry Letters, 2019) Bianco, Valentino; Alonso-Navarro, Miren; Di Silvio, Desire; Moya, Sergio; Cortajarena L., Aitziber; Coluzza, IvanWe present a computational and experimental study on the folding and aggregation in solutions of multiple protein mixtures at different concentrations. We show how in protein mixtures, each component is capable of maintaining its folded state at desensitises higher then the one at which they would precipitate in single species solutions. We demonstrate the generality of our observation over many different proteins using computer simulations capable of fully characterising the cross-aggregation phase diagram of all the mixtures. Dynamic light Scattering experiments were performed to evaluate the aggregation of two proteins, the bovine serum albumin (BSA) and the consensus tetratricopeptide repeat (CTPR), in solutions of one or both proteins. The experiment confirm our hypothesis and the simulations. These findings elucidate critical aspects on the cross-regulation of expression and aggregation of proteins exerted by the cell and on the evolutionary selection of folding and not-aggregating protein sequences, paving the way for new experimental tests.Item In silico evidence that protein unfolding is as a precursor of the protein aggregation(ChemPhysChem, 2019) Bianco, Valentino; Franzese, Giancarlo; Coluzza, IvanWe present a computational study on the folding and aggregation of proteins in an aqueous environment, as a function of its concentration. We show how the increase of the concentration of individual protein species can induce a partial unfolding of the native conformation without the occurrence of aggregates. A further increment of the protein concentration results in the complete loss of the folded structures and induces the formation of protein aggregates. We discuss the effect of the protein interface on the water fluctuations in the protein hydration shell and their relevance in the protein-protein interaction.