Interaction of proteins with polyelectrolytes: comparison of theory to experiment
File(s)
Accepted version
Author(s)
Xu, Xiao
Angioletti-Uberti, Stefano
Lu, Yan
Dzubiella, Joachim
Ballauff, Matthias
Type
Journal Article
Abstract
We discuss recent investigations of the interaction of polyelectrolytes with proteins. In particular, we review our recent studies on the interaction of simple proteins such as human serum albumin (HSA) and lysozyme with linear polyelectrolytes, charged dendrimers, charged networks, and polyelectrolyte brushes. In all cases discussed here, we combined experimental work with molecular dynamics (MD) simulations and mean-field theories. In particular, isothermal titration calorimetry (ITC) has been employed to obtain the respective binding constants Kb and the Gibbs free energy of binding. MD simulations with explicit counterions but implicit water demonstrate that counterion release is the main driving force for the binding of proteins to strongly charged polyelectrolytes: patches of positive charges located on the surface of the protein become multivalent counterions of the polyelectrolyte, thereby releasing a number of counterions condensed on the polyelectrolyte. The binding Gibbs free energy due to counterion release is predicted to scale with the logarithm of the salt concentration in the system, which is verified by both simulations and experiment. In several cases, namely, for the interaction of proteins with linear polyelectrolytes and highly charged hydrophilic dendrimers, the binding constant could be calculated from simulations to very good approximation. This finding demonstrated that in these cases explicit hydration effects do not contribute to the Gibbs free energy of binding. The Gibbs free energy can also be used to predict the kinetics of protein uptake by microgels for a given system by applying dynamic density functional theory. The entire discussion demonstrates that the direct comparison of theory with experiments can lead to a full understanding of the interaction of proteins with charged polymers. Possible implications for applications, such as drug design, are discussed.
Date Issued
2019-04-23
Date Acceptance
2018-08-10
Citation
Langmuir, 2019, 35 (16), pp.5373-5391
ISSN
0743-7463
Publisher
American Chemical Society
Start Page
5373
End Page
5391
Journal / Book Title
Langmuir
Volume
35
Issue
16
Copyright Statement
© 2018 American Chemical Society. This document is the Accepted Manuscript version of a Published Work that appeared in final form in Langmuir, after peer review and technical editing by the publisher. To access the final edited and published work see https://dx.doi.org/10.1021/acs.langmuir.8b01802.
Identifier
https://www.ncbi.nlm.nih.gov/pubmed/30095921
Subjects
Science & Technology
Physical Sciences
Technology
Chemistry, Multidisciplinary
Chemistry, Physical
Materials Science, Multidisciplinary
Chemistry
Materials Science
BOVINE SERUM-ALBUMIN
COUNTERION CONDENSATION
COMPETITIVE ADSORPTION
RECEPTOR-BINDING
UREMIC TOXINS
BRUSHES
RELEASE
THERMODYNAMICS
NANOPARTICLE
DENDRIMERS
MD Multidisciplinary
Chemical Physics
Publication Status
Published
Coverage Spatial
United States
Date Publish Online
2018-08-10