Competing Salt Effects on Phase Behavior of Protein Solutions: Tailoring of Protein Interaction by the Binding of Multivalent Ions and Charge Screening
- Publikationstyp:
- Zeitschriftenaufsatz
- Metadaten:
-
- Autoren
- Elena Jordan
- Felix Roosen-Runge
- Sara Leibfarth
- Fajun Zhang
- Michael Sztucki
- Andreas Hildebrandt
- Oliver Kohlbacher
- Frank Schreiber
- Autoren-URL
- https://www.webofscience.com/api/gateway?GWVersion=2&SrcApp=fis-test-1&SrcAuth=WosAPI&KeyUT=WOS:000342396000033&DestLinkType=FullRecord&DestApp=WOS_CPL
- DOI
- 10.1021/jp5058622
- Externe Identifier
- Clarivate Analytics Document Solution ID: AP9JL
- PubMed Identifier: 25180816
- ISSN
- 1520-6106
- Ausgabe der Veröffentlichung
- 38
- Zeitschrift
- JOURNAL OF PHYSICAL CHEMISTRY B
- Paginierung
- 11365 - 11374
- Datum der Veröffentlichung
- 2014
- Status
- Published
- Titel
- Competing Salt Effects on Phase Behavior of Protein Solutions: Tailoring of Protein Interaction by the Binding of Multivalent Ions and Charge Screening
- Sub types
- Article
- Ausgabe der Zeitschrift
- 118
Datenquelle: Web of Science (Lite)
- Andere Metadatenquellen:
-
- Autoren
- Elena Jordan
- Felix Roosen-Runge
- Sara Leibfarth
- Fajun Zhang
- Michael Sztucki
- Andreas Hildebrandt
- Oliver Kohlbacher
- Frank Schreiber
- DOI
- 10.1021/jp5058622
- eISSN
- 1520-5207
- ISSN
- 1520-6106
- Ausgabe der Veröffentlichung
- 38
- Zeitschrift
- The Journal of Physical Chemistry B
- Sprache
- en
- Online publication date
- 2014
- Paginierung
- 11365 - 11374
- Datum der Veröffentlichung
- 2014
- Status
- Published
- Herausgeber
- American Chemical Society (ACS)
- Herausgeber URL
- http://dx.doi.org/10.1021/jp5058622
- Datum der Datenerfassung
- 2023
- Titel
- Competing Salt Effects on Phase Behavior of Protein Solutions: Tailoring of Protein Interaction by the Binding of Multivalent Ions and Charge Screening
- Ausgabe der Zeitschrift
- 118
Datenquelle: Crossref
- Abstract
- The phase behavior of protein solutions is affected by additives such as crowder molecules or salts. In particular, upon addition of multivalent counterions, a reentrant condensation can occur; i.e., protein solutions are stable for low and high multivalent ion concentrations but aggregating at intermediate salt concentrations. The addition of monovalent ions shifts the phase boundaries to higher multivalent ion concentrations. This effect is found to be reflected in the protein interactions, as accessed via small-angle X-ray scattering. Two simulation schemes (a Monte Carlo sampling of the counterion binding configurations using the detailed protein structure and an analytical coarse-grained binding model) reproduce the shifts of the experimental phase boundaries. The results support a consistent picture of the protein interactions responsible for the phase behavior. The repulsive Coulomb interaction is varied by the binding of multivalent counterions and additionally screened by any increase of the ionic strength. The attractive interaction is induced by the binding of multivalent ions, most likely due to ion bridging between protein molecules. The overall picture of these competing interactions provides interesting insight into possible mechanisms for tailoring interactions in solutions via salt effects.
- Addresses
- Institut für Angewandte Physik, Universität Tübingen , Auf der Morgenstelle 10, 72076 Tübingen, Germany.
- Autoren
- Elena Jordan
- Felix Roosen-Runge
- Sara Leibfarth
- Fajun Zhang
- Michael Sztucki
- Andreas Hildebrandt
- Oliver Kohlbacher
- Frank Schreiber
- DOI
- 10.1021/jp5058622
- eISSN
- 1520-5207
- Externe Identifier
- PubMed Identifier: 25180816
- Funding acknowledgements
- Deutsche Forschungsgemeinschaft:
- Studienstiftung des Deutschen Volkes:
- Open access
- false
- ISSN
- 1520-6106
- Ausgabe der Veröffentlichung
- 38
- Zeitschrift
- The journal of physical chemistry. B
- Schlüsselwörter
- Humans
- Ions
- Salts
- Serum Albumin
- X-Ray Diffraction
- Osmolar Concentration
- Scattering, Small Angle
- Sprache
- eng
- Medium
- Print-Electronic
- Online publication date
- 2014
- Paginierung
- 11365 - 11374
- Datum der Veröffentlichung
- 2014
- Status
- Published
- Datum der Datenerfassung
- 2014
- Titel
- Competing salt effects on phase behavior of protein solutions: tailoring of protein interaction by the binding of multivalent ions and charge screening.
- Sub types
- Research Support, Non-U.S. Gov't
- Journal Article
- Ausgabe der Zeitschrift
- 118
Datenquelle: Europe PubMed Central
- Abstract
- The phase behavior of protein solutions is affected by additives such as crowder molecules or salts. In particular, upon addition of multivalent counterions, a reentrant condensation can occur; i.e., protein solutions are stable for low and high multivalent ion concentrations but aggregating at intermediate salt concentrations. The addition of monovalent ions shifts the phase boundaries to higher multivalent ion concentrations. This effect is found to be reflected in the protein interactions, as accessed via small-angle X-ray scattering. Two simulation schemes (a Monte Carlo sampling of the counterion binding configurations using the detailed protein structure and an analytical coarse-grained binding model) reproduce the shifts of the experimental phase boundaries. The results support a consistent picture of the protein interactions responsible for the phase behavior. The repulsive Coulomb interaction is varied by the binding of multivalent counterions and additionally screened by any increase of the ionic strength. The attractive interaction is induced by the binding of multivalent ions, most likely due to ion bridging between protein molecules. The overall picture of these competing interactions provides interesting insight into possible mechanisms for tailoring interactions in solutions via salt effects.
- Autoren
- Elena Jordan
- Felix Roosen-Runge
- Sara Leibfarth
- Fajun Zhang
- Michael Sztucki
- Andreas Hildebrandt
- Oliver Kohlbacher
- Frank Schreiber
- Autoren-URL
- https://www.ncbi.nlm.nih.gov/pubmed/25180816
- DOI
- 10.1021/jp5058622
- eISSN
- 1520-5207
- Ausgabe der Veröffentlichung
- 38
- Zeitschrift
- J Phys Chem B
- Schlüsselwörter
- Humans
- Ions
- Osmolar Concentration
- Salts
- Scattering, Small Angle
- Serum Albumin
- X-Ray Diffraction
- Sprache
- eng
- Country
- United States
- Paginierung
- 11365 - 11374
- Datum der Veröffentlichung
- 2014
- Status
- Published
- Datum, an dem der Datensatz öffentlich gemacht wurde
- 2015
- Titel
- Competing salt effects on phase behavior of protein solutions: tailoring of protein interaction by the binding of multivalent ions and charge screening.
- Sub types
- Journal Article
- Research Support, Non-U.S. Gov't
- Ausgabe der Zeitschrift
- 118
Datenquelle: PubMed
- Autoren
- Elena Jordan
- Felix Roosen-Runge
- Sara Leibfarth
- Fajun Zhang
- Michael Sztucki
- Andreas Hildebrandt
- Oliver Kohlbacher
- Frank Schreiber
- Zeitschrift
- The Journal of Physical Chemistry B
- Artikelnummer
- 38
- Paginierung
- 11365 - 11374
- Datum der Veröffentlichung
- 2014
- Herausgeber
- American Chemical Society
- Datum der Datenerfassung
- 2020
- Titel
- Competing Salt Effects on Phase Behavior of Protein Solutions: Tailoring of Protein Interaction by the Binding of Multivalent Ions and Charge Screening
- Sub types
- article
- Ausgabe der Zeitschrift
- 118
Datenquelle: Manual
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