Anisotropic protein-protein interactions in dilute and concentrated solutions.

Autor: Pasquier C; ICSM, CNRS, CEA, Univ Montpellier, ENSCM, Marcoule, France; Division of Theoretical Chemistry, Lund University, POB 124, SE-221 00 Lund, Sweden. Electronic address: coralie.pasquier@teokem.lu.se., Midtgaard SR; X-ray and Neutron Science, Niels Bohr Institute, University of Copenhagen, Denmark., Polimeni M; Division of Theoretical Chemistry, Lund University, POB 124, SE-221 00 Lund, Sweden., Jørgensen CI; Novozymes A/S, Denmark., Arleth L; X-ray and Neutron Science, Niels Bohr Institute, University of Copenhagen, Denmark. Electronic address: arleth@nbi.ku.dk., Callisen TH; Division of Theoretical Chemistry, Lund University, POB 124, SE-221 00 Lund, Sweden., Lund M; Division of Theoretical Chemistry, Lund University, POB 124, SE-221 00 Lund, Sweden; LINXS - Lund Institute of Advanced Neutron and X-ray Science, Scheelevägen 19, SE-223 70 Lund, Sweden. Electronic address: mikael.lund@teokem.lu.se.
Jazyk: angličtina
Zdroj: Journal of colloid and interface science [J Colloid Interface Sci] 2023 Jan; Vol. 629 (Pt A), pp. 794-804. Date of Electronic Publication: 2022 Aug 29.
DOI: 10.1016/j.jcis.2022.08.054
Abstrakt: Interactions between biomolecules are ubiquitous in nature and crucial to many applications including vaccine development; environmentally friendly textile detergents; and food formulation. Using small angle X-ray scattering and structure-based molecular simulations, we explore protein-protein interactions in dilute to semi-concentrated protein solutions. We address the pertinent question, whether interaction models developed at infinite dilution can be extrapolated to concentrated regimes? Our analysis is based on measured and simulated osmotic second virial coefficients and solution structure factors at varying protein concentration and for different variants of the protein Thermomyces Lanuginosus Lipase (TLL). We show that in order to span the dilute and semi-concentrated regime, any model must carefully capture the balance between spatial and orientational correlations as the protein concentration is elevated. This requires consideration of the protein surface morphology, including possible patch interactions. Experimental data for TLL is most accurately described when assuming a patchy interaction, leading to dimer formation. Our analysis supports that the dimeric proteins predominantly exist in their open conformation where the active site is exposed, thereby maximising hydrophobic attractions that promote inter-protein alignment.
Competing Interests: Declaration of Competing Interest The authors declare that they have no known competing financial interests or personal relationships that could have appeared to influence the work reported in this paper.
(Copyright © 2022 The Authors. Published by Elsevier Inc. All rights reserved.)
Databáze: MEDLINE
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