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Cation-Induced Hydration Effects Cause Lower Critical Solution Temperature Behavior in Protein Solutions

Matsarskaia, Olga ; Braun, Michal K. ; Roosen-Runge, Felix LU ; Wolf, Marcell ; Zhang, Fajun ; Roth, Roland and Schreiber, Frank (2016) In Journal of Physical Chemistry B 120(31). p.7731-7736
Abstract

The phase behavior of protein solutions is important for numerous phenomena in biology and soft matter. We report a lower critical solution temperature (LCST) phase behavior of aqueous solutions of a globular protein induced by multivalent metal ions around physiological temperatures. The LCST behavior manifests itself via a liquid-liquid phase separation of the protein-salt solution upon heating. Isothermal titration calorimetry and zeta-potential measurements indicate that here cation-protein binding is an endothermic, entropy-driven process. We offer a mechanistic explanation of the LCST. First, cations bind to protein surface groups driven by entropy changes of hydration water. Second, the bound cations bridge to other protein... (More)

The phase behavior of protein solutions is important for numerous phenomena in biology and soft matter. We report a lower critical solution temperature (LCST) phase behavior of aqueous solutions of a globular protein induced by multivalent metal ions around physiological temperatures. The LCST behavior manifests itself via a liquid-liquid phase separation of the protein-salt solution upon heating. Isothermal titration calorimetry and zeta-potential measurements indicate that here cation-protein binding is an endothermic, entropy-driven process. We offer a mechanistic explanation of the LCST. First, cations bind to protein surface groups driven by entropy changes of hydration water. Second, the bound cations bridge to other protein molecules, inducing an entropy-driven attraction causing the LCST. Our findings have general implications for condensation, LCST, and hydration behavior of (bio)polymer solutions as well as the understanding of biological effects of (heavy) metal ions and their hydration.

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author
; ; ; ; ; and
publishing date
type
Contribution to journal
publication status
published
in
Journal of Physical Chemistry B
volume
120
issue
31
pages
6 pages
publisher
The American Chemical Society (ACS)
external identifiers
  • scopus:84982085673
  • pmid:27414502
ISSN
1520-6106
DOI
10.1021/acs.jpcb.6b04506
language
English
LU publication?
no
id
1716a747-364a-4ad7-8129-db335dfb721a
date added to LUP
2018-12-17 09:39:25
date last changed
2024-09-17 10:03:54
@article{1716a747-364a-4ad7-8129-db335dfb721a,
  abstract     = {{<p>The phase behavior of protein solutions is important for numerous phenomena in biology and soft matter. We report a lower critical solution temperature (LCST) phase behavior of aqueous solutions of a globular protein induced by multivalent metal ions around physiological temperatures. The LCST behavior manifests itself via a liquid-liquid phase separation of the protein-salt solution upon heating. Isothermal titration calorimetry and zeta-potential measurements indicate that here cation-protein binding is an endothermic, entropy-driven process. We offer a mechanistic explanation of the LCST. First, cations bind to protein surface groups driven by entropy changes of hydration water. Second, the bound cations bridge to other protein molecules, inducing an entropy-driven attraction causing the LCST. Our findings have general implications for condensation, LCST, and hydration behavior of (bio)polymer solutions as well as the understanding of biological effects of (heavy) metal ions and their hydration.</p>}},
  author       = {{Matsarskaia, Olga and Braun, Michal K. and Roosen-Runge, Felix and Wolf, Marcell and Zhang, Fajun and Roth, Roland and Schreiber, Frank}},
  issn         = {{1520-6106}},
  language     = {{eng}},
  month        = {{08}},
  number       = {{31}},
  pages        = {{7731--7736}},
  publisher    = {{The American Chemical Society (ACS)}},
  series       = {{Journal of Physical Chemistry B}},
  title        = {{Cation-Induced Hydration Effects Cause Lower Critical Solution Temperature Behavior in Protein Solutions}},
  url          = {{http://dx.doi.org/10.1021/acs.jpcb.6b04506}},
  doi          = {{10.1021/acs.jpcb.6b04506}},
  volume       = {{120}},
  year         = {{2016}},
}