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Strong Isotope Effects on Effective Interactions and Phase Behavior in Protein Solutions in the Presence of Multivalent Ions

Braun, Michal K. ; Wolf, Marcell ; Matsarskaia, Olga ; da Vela, Stefano ; Roosen-Runge, Felix LU ; Sztucki, Michael ; Roth, Roland ; Zhang, Fajun and Schreiber, Frank (2017) In The Journal of Physical Chemistry Part B 121. p.1731-1731
Abstract
In this article, we have studied the influence of the isotopic composition of the solvent (H2O or D2O) on the effective interactions and the phase behavior of the globular protein bovine serum albumin in solution with two trivalent salts (LaCl3 and YCl3). Protein solutions with both salts exhibit a reentrant condensation phase behavior. The condensed regime (regime II) in between two salt concentration boundaries (c* < cs < c**) is significantly broadened by replacing H2O with D2O. Within regime II, liquid–liquid phase separation (LLPS) occurs. The samples that undergo LLPS have a lower critical solution temperature (LCST). The value of LCST decreases significantly with increasing solvent fraction of D2O. The effective... (More)
In this article, we have studied the influence of the isotopic composition of the solvent (H2O or D2O) on the effective interactions and the phase behavior of the globular protein bovine serum albumin in solution with two trivalent salts (LaCl3 and YCl3). Protein solutions with both salts exhibit a reentrant condensation phase behavior. The condensed regime (regime II) in between two salt concentration boundaries (c* < cs < c**) is significantly broadened by replacing H2O with D2O. Within regime II, liquid–liquid phase separation (LLPS) occurs. The samples that undergo LLPS have a lower critical solution temperature (LCST). The value of LCST decreases significantly with increasing solvent fraction of D2O. The effective protein–protein interactions characterized by small-angle X-ray scattering demonstrate that although changing the solvent has negligible effects below c*, where the interactions are dominated by electrostatic repulsion, an enhanced effective attraction is observed in D2O above c*, consistent with the phase behavior observed. As the LCST–LLPS is an entropy-driven phase transition, the results of this study emphasize the role of entropy in solvent isotope effects. (Less)
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author
; ; ; ; ; ; ; and
publishing date
type
Contribution to journal
publication status
published
in
The Journal of Physical Chemistry Part B
volume
121
pages
1739 pages
publisher
The American Chemical Society (ACS)
external identifiers
  • pmid:28191978
  • scopus:85027245454
ISSN
1520-5207
DOI
10.1021/acs.jpcb.6b12814
language
English
LU publication?
no
id
f7307fd6-de1a-4187-8d22-597f47e82ee2
date added to LUP
2018-12-17 09:34:50
date last changed
2022-04-25 19:56:22
@article{f7307fd6-de1a-4187-8d22-597f47e82ee2,
  abstract     = {{In this article, we have studied the influence of the isotopic composition of the solvent (H2O or D2O) on the effective interactions and the phase behavior of the globular protein bovine serum albumin in solution with two trivalent salts (LaCl3 and YCl3). Protein solutions with both salts exhibit a reentrant condensation phase behavior. The condensed regime (regime II) in between two salt concentration boundaries (c* &lt; cs &lt; c**) is significantly broadened by replacing H2O with D2O. Within regime II, liquid–liquid phase separation (LLPS) occurs. The samples that undergo LLPS have a lower critical solution temperature (LCST). The value of LCST decreases significantly with increasing solvent fraction of D2O. The effective protein–protein interactions characterized by small-angle X-ray scattering demonstrate that although changing the solvent has negligible effects below c*, where the interactions are dominated by electrostatic repulsion, an enhanced effective attraction is observed in D2O above c*, consistent with the phase behavior observed. As the LCST–LLPS is an entropy-driven phase transition, the results of this study emphasize the role of entropy in solvent isotope effects.}},
  author       = {{Braun, Michal K. and Wolf, Marcell and Matsarskaia, Olga and da Vela, Stefano and Roosen-Runge, Felix and Sztucki, Michael and Roth, Roland and Zhang, Fajun and Schreiber, Frank}},
  issn         = {{1520-5207}},
  language     = {{eng}},
  pages        = {{1731--1731}},
  publisher    = {{The American Chemical Society (ACS)}},
  series       = {{The Journal of Physical Chemistry Part B}},
  title        = {{Strong Isotope Effects on Effective Interactions and Phase Behavior in Protein Solutions in the Presence of Multivalent Ions}},
  url          = {{http://dx.doi.org/10.1021/acs.jpcb.6b12814}},
  doi          = {{10.1021/acs.jpcb.6b12814}},
  volume       = {{121}},
  year         = {{2017}},
}