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• W1978649813 abstract "The role of intermolecular interaction in fibril-forming protein solutions and its relation with molecular conformation is a crucial aspect for the control and inhibition of amyloid structures. Here, we use optical spectroscopies, x-ray and light scattering to study the fibril formation and the protein-protein interactions of different model proteins. In the case of lysozyme, the monomeric solution is kept in a thermodynamically metastable state by strong electrostatic repulsion, even in denaturing conditions. At high temperature proteins are driven out of metastability through conformational sub-states, which are kinetically populated and experience lower activation energy for fibril formation. This explains how electrostatic repulsion may act as a gatekeeper in selecting the appropriate pathway to fibrillation. The protein density fluctuations are measured by light scattering and exhibit a regime dominated by protein concentration. Highly charged colloidal solutions are characterized by damped density fluctuations and mimics locally a crowded environment. Further, by photon correlation spectroscopy (PCS) and fluorescence correlation spectroscopy (FCS) we measure protein collective and self-diffusion. Both PCS and FCS evidence how an increase of concentration hinders protein self-diffusion, likely due to both hydrodynamics and crowding effect." @default.
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• W1978649813 date "2015-01-01" @default.
• W1978649813 modified "2023-09-30" @default.
• W1978649813 title "Electrostatics Promotes Molecular Crowding and Selects the Fibrillation Pathway in Fibril-Forming Protein Solutions" @default.
• W1978649813 doi "https://doi.org/10.1016/j.bpj.2014.11.2866" @default.
• W1978649813 hasPublicationYear "2015" @default.
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