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Like-charged protein-polyelectrolyte complexation driven by charge patches.

Authors :
Yigit C
Heyda J
Ballauff M
Dzubiella J
Source :
The Journal of chemical physics [J Chem Phys] 2015 Aug 14; Vol. 143 (6), pp. 064905.
Publication Year :
2015

Abstract

We study the pair complexation of a single, highly charged polyelectrolyte (PE) chain (of 25 or 50 monomers) with like-charged patchy protein models (CPPMs) by means of implicit-solvent, explicit-salt Langevin dynamics computer simulations. Our previously introduced set of CPPMs embraces well-defined zero-, one-, and two-patched spherical globules each of the same net charge and (nanometer) size with mono- and multipole moments comparable to those of globular proteins with similar size. We observe large binding affinities between the CPPM and the like-charged PE in the tens of the thermal energy, kBT, that are favored by decreasing salt concentration and increasing charge of the patch(es). Our systematic analysis shows a clear correlation between the distance-resolved potentials of mean force, the number of ions released from the PE, and CPPM orientation effects. In particular, we find a novel two-site binding behavior for PEs in the case of two-patched CPPMs, where intermediate metastable complex structures are formed. In order to describe the salt-dependence of the binding affinity for mainly dipolar (one-patched) CPPMs, we introduce a combined counterion-release/Debye-Hückel model that quantitatively captures the essential physics of electrostatic complexation in our systems.

Details

Language :
English
ISSN :
1089-7690
Volume :
143
Issue :
6
Database :
MEDLINE
Journal :
The Journal of chemical physics
Publication Type :
Academic Journal
Accession number :
26277164
Full Text :
https://doi.org/10.1063/1.4928078