Cation-Induced Hydration Effects Cause Lower Critical Solution Temperature Behavior in Protein Solutions
(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
- Matsarskaia, Olga ; Braun, Michal K. ; Roosen-Runge, Felix LU ; Wolf, Marcell ; Zhang, Fajun ; Roth, Roland and Schreiber, Frank
- publishing date
- 2016-08-11
- 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
-
- pmid:27414502
- scopus:84982085673
- 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
- 2024-10-01 12:41:46
@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}}, }