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Proteins and polyelectrolytes: A charged relationship

Authors
Journal
Current Opinion in Colloid & Interface Science
1359-0294
Publisher
Elsevier
Volume
17
Issue
2
Identifiers
DOI: 10.1016/j.cocis.2011.10.001
Keywords
  • Polyelectrolyte
  • Polyelectrolyte Brush
  • Charged Gel
  • Counterion Release
  • Protein
Disciplines
  • Biology

Abstract

Abstract We review the interaction of charged polymeric systems with proteins. In solutions of low ionic strength there are many examples of proteins attracted to polyelectrolytes even if both systems carry the same overall charge. This attractive interaction is widespread, having been observed for single polyelectrolyte chains as well as for polyelectrolytes grafted to surfaces (polyelectrolyte brushes) and charged polymeric networks. In all cases, adding salt weakens the interaction considerably. We discuss the suggestion that the attractive force at low salinity originates from the asymmetry of interaction between charged polymer segments and charged patches on the surface of the protein globule. This can be explained if the attractive force is mainly due to a counterion release force, i.e., the polyelectrolyte chains become the multivalent counterions for the patches of opposite charge localized on the surface of the proteins. We review a selection of simple models that lead to semi-quantitative estimates of this force as the function of salt concentration.

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