Raccosta, S. and Blanco, M. and Roberts, C. J. and Martorana, V. and Manno, M. (2016) Electrostatics promotes molecular crowding and selects the aggregation pathway in fibril-forming protein solutions. Il nuovo cimento C, 39 (3). pp. 1-9. ISSN 1826-9885
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Abstract
The role of intermolecular interaction in fibril-forming protein solutions and its relation with molecular conformation are crucial aspects for the control and inhibition of amyloid structures. Here, we study the fibril formation and the protein-protein interactions for two proteins at acidic pH, lysozyme and α-chymotrypsinogen. By using light scattering experiments and the Kirkwood-Buff integral approach, we show how concentration fluctuations are damped even at moderate protein concentrations by the dominant long-ranged electrostatic repulsion, which determines an effective crowded environment. In denaturing conditions, electrostatic repulsion keeps the monomeric solution in a thermodynamically metastable state, which is escaped through kinetically populated conformational sub-states. This explains how electrostatics acts as a gatekeeper in selecting a specific aggregation pathway.
| Item Type: | Article |
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| Subjects: | 500 Scienze naturali e Matematica > 530 Fisica |
| Depositing User: | Marina Spanti |
| Date Deposited: | 29 Sep 2020 16:17 |
| Last Modified: | 29 Sep 2020 16:17 |
| URI: | http://eprints.bice.rm.cnr.it/id/eprint/19300 |
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