| Article ID | Journal | Published Year | Pages | File Type |
|---|---|---|---|---|
| 603442 | Current Opinion in Colloid & Interface Science | 2012 | 7 Pages |
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.
Graphical abstractFigure optionsDownload full-size imageDownload high-quality image (194 K)Download as PowerPoint slideHighlights► Role of charges for the interaction of proteins with charged polymeric systems. ► Attractive forces exist also between like charged proteins and polymeric systems. ► Strong attraction at low ionic strength is caused by the counterion release force. ► Proteins interact stronger with polymer brushes than with linear polyelectrolytes.
