Journal Article FZJ-2021-05929

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Interactions in protein solutions close to liquid–liquid phase separation: ethanol reduces attractions via changes of the dielectric solution properties

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2021
RSC Publ. Cambridge

Physical chemistry, chemical physics 23(39), 22384 - 22394 () [10.1039/D1CP03210K]

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Abstract: Ethanol is a common protein crystallization agent, precipitant, and denaturant, but also alters the dielectric properties of solutions. While ethanol-induced unfolding is largely ascribed to its hydrophobic parts, its effect on protein phase separation and inter-protein interactions remains poorly understood. Here, the effects of ethanol and NaCl on the phase behavior and interactions of protein solutions are studied in terms of the metastable liquid–liquid phase separation (LLPS) and the second virial coefficient B2 using lysozyme solutions. Determination of the phase diagrams shows that the cloud-point temperatures are reduced and raised by the addition of ethanol and salt, respectively. The observed trends can be explained using the extended law of corresponding states as changes of B2. The results for B2 agree quantitatively with those of static light scattering and small-angle X-ray scattering experiments. Furthermore, B2 values calculated based on inter-protein interactions described by the Derjaguin-Landau-Verwey-Overbeek (DLVO) potential and considering the dielectric solution properties and electrostatic screening due to the ethanol and salt content quantitatively agree with the experimentally observed B2 values.

Classification:

Contributing Institute(s):
  1. Biomakromolekulare Systeme und Prozesse (IBI-4)
Research Program(s):
  1. 5241 - Molecular Information Processing in Cellular Systems (POF4-524) (POF4-524)

Appears in the scientific report 2021
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Medline ; Creative Commons Attribution-NonCommercial CC BY-NC 3.0 ; OpenAccess ; Allianz-Lizenz / DFG ; Clarivate Analytics Master Journal List ; Current Contents - Physical, Chemical and Earth Sciences ; Essential Science Indicators ; IF < 5 ; JCR ; National-Konsortium ; NationallizenzNationallizenz ; SCOPUS ; Science Citation Index Expanded ; Web of Science Core Collection
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Open Access

 Datensatz erzeugt am 2021-12-27, letzte Änderung am 2022-01-31


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