Understanding the Interaction of Polyelectrolyte Architectures with Proteins and Biosystems
Open Access
- 26 June 2020
- journal article
- review article
- Published by Wiley in Angewandte Chemie-International Edition
- Vol. 60 (8), 3882-3904
- https://doi.org/10.1002/anie.202006457
Abstract
Polyelectrolytes such as e.g. DNA or heparin are long linear or branched macromolecules onto which charges are appended. The counterions neutralizing these charges may dissociate in water and will largely determine the interaction of such polyelectrolytes with biomolecules and in particular with proteins. Here we review studies on the interaction of proteins with polyelectrolytes and how this knowledge can be used for medical applications. Counterion release was identified as the main driving force for the binding of proteins to polyelectrolytes: Patches of positive charge become multivalent counterions of the polyelectrolyte which leads to the release of counterions of the polyelectrolyte and a concomitant increase of entropy. We show this by surveying investigations done on the interaction of proteins with natural and synthetic polyelectrolytes. Special emphasis is laid on sulfated dendritic polyglycerols (dPGS). The entire overview demonstrates that we are moving on to a better understanding of charge‐charge interaction in system of biological relevance. Hence, research along these lines will aid and promote the design of synthetic polyelectrolytes for medical applications.Keywords
Funding Information
- Canadian Institutes of Health Research (MOP-119425)
- Natural Sciences and Engineering Research Council of Canada (RGPIN 2020-07011)
- Michael Smith Foundation for Health Research
- Deutsche Forschungsgemeinschaft (IRTG 1524, SFB 765)
- Canada Foundation for Innovation
- Canada Research Chairs (Tier 1)
This publication has 247 references indexed in Scilit:
- Binding of the Dimeric Deinococcus radiodurans Single-Stranded DNA Binding Protein to Single-Stranded DNABiochemistry, 2010
- Complement: a key system for immune surveillance and homeostasisNature Immunology, 2010
- Thermodynamics of the DNA Structural Selectivity of the Pol I DNA Polymerases from Escherichia coli and Thermus aquaticusBiophysical Journal, 2010
- Nanogels as Pharmaceutical Carriers: Finite Networks of Infinite CapabilitiesAngewandte Chemie-International Edition, 2009
- Peptide adsorption on a hydrophobic surface results from an interplay of solvation, surface, and intrapeptide forcesProceedings of the National Academy of Sciences, 2008
- Triggers, targets and treatments for thrombosisNature, 2008
- Formation of a Wrapped DNA–Protein Interface: Experimental Characterization and Analysis of the Large Contributions of Ions and Water to the Thermodynamics of Binding IHF to H′ DNAJournal of Molecular Biology, 2007
- What Drives Proteins into the Major or Minor Grooves of DNA?Journal of Molecular Biology, 2006
- Saccharomyces cerevisiae Replication Protein A Binds to Single-Stranded DNA in Multiple Salt-Dependent ModesBiochemistry, 2006
- Effects of Monovalent Anions on a Temperature-Dependent Heat Capacity Change for Escherichia coli SSB Tetramer Binding to Single-Stranded DNABiochemistry, 2006