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Short-Time Transport Properties of Bidisperse Suspensions of Immunoglobulins and Serum Albumins Consistent with a Colloid Physics Picture

Beck, Christian ; Grimaldo, Marco ; Lopez, Hender ; Da Vela, Stefano ; Sohmen, Benedikt ; Zhang, Fajun LU ; Oettel, Martin ; Barrat, Jean Louis ; Roosen-Runge, Felix LU and Schreiber, Frank , et al. (2022) In Journal of Physical Chemistry B 126(38). p.7400-7408
Abstract

The crowded environment of biological systems such as the interior of living cells is occupied by macromolecules with a broad size distribution. This situation of polydispersity might influence the dependence of the diffusive dynamics of a given tracer macromolecule in a monodisperse solution on its hydrodynamic size and on the volume fraction. The resulting size dependence of diffusive transport crucially influences the function of a living cell. Here, we investigate a simplified model system consisting of two constituents in aqueous solution, namely, of the proteins bovine serum albumin (BSA) and bovine polyclonal gamma-globulin (Ig), systematically depending on the total volume fraction and ratio of these constituents. From... (More)

The crowded environment of biological systems such as the interior of living cells is occupied by macromolecules with a broad size distribution. This situation of polydispersity might influence the dependence of the diffusive dynamics of a given tracer macromolecule in a monodisperse solution on its hydrodynamic size and on the volume fraction. The resulting size dependence of diffusive transport crucially influences the function of a living cell. Here, we investigate a simplified model system consisting of two constituents in aqueous solution, namely, of the proteins bovine serum albumin (BSA) and bovine polyclonal gamma-globulin (Ig), systematically depending on the total volume fraction and ratio of these constituents. From high-resolution quasi-elastic neutron spectroscopy, the separate apparent short-time diffusion coefficients for BSA and Ig in the mixture are extracted, which show substantial deviations from the diffusion coefficients measured in monodisperse solutions at the same total volume fraction. These deviations can be modeled quantitatively using results from the short-time rotational and translational diffusion in a two-component hard sphere system with two distinct, effective hydrodynamic radii. Thus, we find that a simple colloid picture well describes short-time diffusion in binary mixtures as a function of the mixing ratio and the total volume fraction. Notably, the self-diffusion of the smaller protein BSA in the mixture is faster than the diffusion in a pure BSA solution, whereas the self-diffusion of Ig in the mixture is slower than in the pure Ig solution.

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publishing date
type
Contribution to journal
publication status
published
in
Journal of Physical Chemistry B
volume
126
issue
38
pages
9 pages
publisher
The American Chemical Society (ACS)
external identifiers
  • pmid:36112146
  • scopus:85138811832
ISSN
1520-6106
DOI
10.1021/acs.jpcb.2c02380
language
English
LU publication?
no
id
425496b1-6065-4c85-b103-da0e7fb4d645
date added to LUP
2023-08-14 10:28:53
date last changed
2024-04-20 00:30:47
@article{425496b1-6065-4c85-b103-da0e7fb4d645,
  abstract     = {{<p>The crowded environment of biological systems such as the interior of living cells is occupied by macromolecules with a broad size distribution. This situation of polydispersity might influence the dependence of the diffusive dynamics of a given tracer macromolecule in a monodisperse solution on its hydrodynamic size and on the volume fraction. The resulting size dependence of diffusive transport crucially influences the function of a living cell. Here, we investigate a simplified model system consisting of two constituents in aqueous solution, namely, of the proteins bovine serum albumin (BSA) and bovine polyclonal gamma-globulin (Ig), systematically depending on the total volume fraction and ratio of these constituents. From high-resolution quasi-elastic neutron spectroscopy, the separate apparent short-time diffusion coefficients for BSA and Ig in the mixture are extracted, which show substantial deviations from the diffusion coefficients measured in monodisperse solutions at the same total volume fraction. These deviations can be modeled quantitatively using results from the short-time rotational and translational diffusion in a two-component hard sphere system with two distinct, effective hydrodynamic radii. Thus, we find that a simple colloid picture well describes short-time diffusion in binary mixtures as a function of the mixing ratio and the total volume fraction. Notably, the self-diffusion of the smaller protein BSA in the mixture is faster than the diffusion in a pure BSA solution, whereas the self-diffusion of Ig in the mixture is slower than in the pure Ig solution.</p>}},
  author       = {{Beck, Christian and Grimaldo, Marco and Lopez, Hender and Da Vela, Stefano and Sohmen, Benedikt and Zhang, Fajun and Oettel, Martin and Barrat, Jean Louis and Roosen-Runge, Felix and Schreiber, Frank and Seydel, Tilo}},
  issn         = {{1520-6106}},
  language     = {{eng}},
  month        = {{09}},
  number       = {{38}},
  pages        = {{7400--7408}},
  publisher    = {{The American Chemical Society (ACS)}},
  series       = {{Journal of Physical Chemistry B}},
  title        = {{Short-Time Transport Properties of Bidisperse Suspensions of Immunoglobulins and Serum Albumins Consistent with a Colloid Physics Picture}},
  url          = {{http://dx.doi.org/10.1021/acs.jpcb.2c02380}},
  doi          = {{10.1021/acs.jpcb.2c02380}},
  volume       = {{126}},
  year         = {{2022}},
}