Effect of Protein Surface Charge Distribution on Protein-Polyelectrolyte Complexation.

Biomacromolecules
Sieun KimBradley D Olsen

Abstract

Charge anisotropy or the presence of charge patches at protein surfaces has long been thought to shift the coacervation curves of proteins and has been used to explain the ability of some proteins to coacervate on the "wrong side" of their isoelectric point. This work makes use of a panel of engineered superfolder green fluorescent protein mutants with varying surface charge distributions but equivalent net charge and a suite of strong and weak polyelectrolytes to explore this concept. A patchiness parameter, which assessed the charge correlation between points on the surface of the protein, was used to quantify the patchiness of the designed mutants. Complexation between the polyelectrolytes and proteins showed that the mutant with the largest patchiness parameter was the most likely to form complexes, while the smallest was the least likely to do so. The patchiness parameter was found to correlate well with the phase behavior of the protein-polymer mixtures, where both macrophase separation and the formation of soluble aggregates were promoted by increasing the patchiness depending on the polyelectrolyte with which the protein was mixed. Increasing total charge and increasing strength of the polyelectrolyte promote interactio...Continue Reading

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Citations

May 1, 2021·Protein Science : a Publication of the Protein Society·Chad M DashnawBryan F Shaw
Jun 22, 2021·Soft Matter·Nicholas A Zervoudis, Allie C Obermeyer
Nov 19, 2020·The Journal of Physical Chemistry. B·Rituparna Samanta, Venkat Ganesan

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