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Sorption and spatial distribution of protein globules in charged hydrogel particles

By Irene Adroher-Benitez, Arturo Moncho-Jorda and Joachim Dzubiella

Abstract

We have theoretically studied the uptake of a non-uniformly charged biomolecule, suitable to represent a globular protein or a drug, by a charged hydrogel carrier in the presence of a 1:1 electrolyte. Based on the analysis of a physical interaction Hamiltonian including monopolar, dipolar and Born (self-energy) contributions derived from linear electrostatic theory of the unperturbed homogeneous hydrogel, we have identified five different sorption states of the system, from complete repulsion of the molecule to its full sorption deep inside the hydrogel, passing through meta- and stable surface adsorption states. The results are summarized in state diagrams that also explore the effects of varying the electrolyte concentration, the sign of the net electric charge of the biomolecule, and the role of including excluded-volume (steric) or hydrophobic biomolecule-hydrogel interactions. We show that the dipole moment of the biomolecule is a key parameter controlling the spatial distribution of the globules. In particular, biomolecules with a large dipole moment tend to be adsorbed at the external surface of the hydrogel, even if like-charged, whereas uniformly charged biomolecules tend to partition towards the internal core of an oppositely-charged hydrogel. Hydrophobic attraction shifts the states towards internal sorption of the biomolecule, whereas steric repulsion promotes surface adsorption for oppositely-charged biomolecules, or the total exclusion for likely-charged ones. Our results establish a guidance for the spatial partitioning of proteins and drugs in hydrogel carriers, tuneable by hydrogel charge, pH and salt concentration.Comment: 16 pages, 5 figure

Topics: Condensed Matter - Soft Condensed Matter, Physics - Chemical Physics
Publisher: 'American Chemical Society (ACS)'
Year: 2017
DOI identifier: 10.1021/acs.langmuir.7b00356
OAI identifier: oai:arXiv.org:1704.07769

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