Anisotropic protein-protein interactions in dilute and concentrated solutions
Pasquier, Coralie LU ; Midtgaard, Søren Roi ; Polimeni, Marco LU ; Jørgensen, Christian Isak LU ; Arleth, Lise ; Callisen, Thomas H. and Lund, Mikael LU
(2023)
In Journal of Colloid and Interface Science
629.
p.794-804
- Abstract
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... (More)
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.
(Less)
- author
- Pasquier, Coralie
LU
; Midtgaard, Søren Roi
; Polimeni, Marco
LU
; Jørgensen, Christian Isak
LU
; Arleth, Lise
; Callisen, Thomas H.
and Lund, Mikael
LU
- organization
- publishing date
- 2023-01
- type
- Contribution to journal
- publication status
- published
- subject
- keywords
- Directional interactions, Molecular modelling, Protein–protein interactions, Small-Angle X-ray Scattering, Solution stability
- in
- Journal of Colloid and Interface Science
- volume
- 629
- pages
- 11 pages
- publisher
- Elsevier
- external identifiers
-
- scopus:85137637518
- pmid:36099847
- ISSN
- 0021-9797
- DOI
- 10.1016/j.jcis.2022.08.054
- language
- English
- LU publication?
- yes
- additional info
- Publisher Copyright: © 2022 The Authors
- id
- a51936bf-a20c-45e1-86fa-11db48a4ec6d
- date added to LUP
- 2022-11-17 17:18:21
- date last changed
- 2024-06-27 15:29:29
@article{a51936bf-a20c-45e1-86fa-11db48a4ec6d,
abstract = {{<p>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 <i>Thermomyces Lanuginosus</i> 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.</p>}},
author = {{Pasquier, Coralie and Midtgaard, Søren Roi and Polimeni, Marco and Jørgensen, Christian Isak and Arleth, Lise and Callisen, Thomas H. and Lund, Mikael}},
issn = {{0021-9797}},
keywords = {{Directional interactions; Molecular modelling; Protein–protein interactions; Small-Angle X-ray Scattering; Solution stability}},
language = {{eng}},
pages = {{794--804}},
publisher = {{Elsevier}},
series = {{Journal of Colloid and Interface Science}},
title = {{Anisotropic protein-protein interactions in dilute and concentrated solutions}},
url = {{http://dx.doi.org/10.1016/j.jcis.2022.08.054}},
doi = {{10.1016/j.jcis.2022.08.054}},
volume = {{629}},
year = {{2023}},
}