Understanding the Interaction of Polyelectrolyte Architectures with Proteins and Biosystems

Angew Chem Int Ed Engl. 2021 Feb 19;60(8):3882-3904. doi: 10.1002/anie.202006457. Epub 2020 Oct 27.

Abstract

The counterions neutralizing the charges on polyelectrolytes such as DNA or heparin may dissociate in water and greatly influence the interaction of such polyelectrolytes with biomolecules, particularly proteins. In this Review we give an overview of 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 and lead to the release of counterions from the polyelectrolyte and a concomitant increase in entropy. This is shown from investigations on the interaction of proteins with natural and synthetic polyelectrolytes. Special emphasis is paid to sulfated dendritic polyglycerols (dPGS). The Review demonstrates that we are moving to a better understanding of charge-charge interactions in systems of biological relevance. Research along these lines will aid and promote the design of synthetic polyelectrolytes for medical applications.

Keywords: complementary binding; counterion release; heparin; inflammation; polyelectrolytes.

Publication types

  • Research Support, Non-U.S. Gov't
  • Review

MeSH terms

  • Antineoplastic Agents / chemistry
  • Antineoplastic Agents / pharmacology
  • Cell Survival / drug effects
  • DNA / chemistry*
  • DNA / metabolism
  • Drug Carriers / chemistry
  • Glycosaminoglycans / chemistry
  • Glycosaminoglycans / metabolism
  • Humans
  • Polyelectrolytes / chemistry*
  • Polyelectrolytes / metabolism
  • Protein Binding
  • Proteins / chemistry*
  • Proteins / metabolism
  • Thermodynamics

Substances

  • Antineoplastic Agents
  • Drug Carriers
  • Glycosaminoglycans
  • Polyelectrolytes
  • Proteins
  • DNA

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