2020
DOI: 10.1039/d0cp03633a
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Charge regulation of colloidal particles in aqueous solutions

Abstract: We study charge regulation of colloidal particles inside aqueous electrolyte solutions. To stabilize colloidal suspension against precipitation, colloidal particles are synthesized with either acidic or basic groups on their surface....

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Cited by 28 publications
(55 citation statements)
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References 90 publications
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“…Specifically, can a protein's net charge (Z) be altered by the charge of its neighbor via charge regulation? [13][14][15] Monte Carlo simulations of protein crowding (at low ionic strength) suggest the answer to be yes. 13 Based upon the role of protein charge in catalysis, molecular recognition, and aggregation, 16,17 these theoretical results suggest that the function or dysfunction of a protein can be controlled by the charge of its neighbors, assuming that they are sufficiently crowded and at low ionic strength.…”
Section: Introductionmentioning
confidence: 99%
See 1 more Smart Citation
“…Specifically, can a protein's net charge (Z) be altered by the charge of its neighbor via charge regulation? [13][14][15] Monte Carlo simulations of protein crowding (at low ionic strength) suggest the answer to be yes. 13 Based upon the role of protein charge in catalysis, molecular recognition, and aggregation, 16,17 these theoretical results suggest that the function or dysfunction of a protein can be controlled by the charge of its neighbors, assuming that they are sufficiently crowded and at low ionic strength.…”
Section: Introductionmentioning
confidence: 99%
“…One question that has been lurking in the field of protein electrostatics, experimentally unanswered, is: how are the electrostatic properties of a protein affected intermolecularly, by the net charge (electric field) of its neighbors in a crowded environment? Specifically, can a protein's net charge ( Z ) be altered by the charge of its neighbor via charge regulation ? 13–15 Monte Carlo simulations of protein crowding (at low ionic strength) suggest the answer to be yes 13 . Based upon the role of protein charge in catalysis, molecular recognition, and aggregation, 16,17 these theoretical results suggest that the function or dysfunction of a protein can be controlled by the charge of its neighbors, assuming that they are sufficiently crowded and at low ionic strength.…”
Section: Introductionmentioning
confidence: 99%
“…For weakly charged surfaces or on sufficiently small length scales, the discreteness of the electric charge will become noticeable. This has inspired a number of authors to compute the electrostatic potential produced by an ordered array of surface charges [19][20][21] or even a single surface charge [22][23][24][25] and others to use virial expansions [26,27] and Monte Carlo simulations [28][29][30][31][32][33][34][35][36][37] to account for charge discreteness. Some studies have focused on the pressure that acts across electrolytes due to the presence of discrete charges [28,35,38], yet-perhaps somewhat surprisingly-there has not been an attempt so far to compute the free energy of a single planar dielectric interface with discrete charges and compare this with the corresponding free energy derived for a continuous charge distribution.…”
Section: Introductionmentioning
confidence: 99%
“…That means differences exist in the potential/charge fields responsible for interactions. Depending on the nature and mechanism of surface charge regulation (Ong et al, 2020;Bakhshandeh, 2020), it is possible to have electrostatic systems with specific ranges of potential, from dilute solutions (Konovalov & Ryzhkina, 2014) with low surface potentials to concentrated solutions with high surface potentials (Wennerström et al, 2017). The former range of potential is the basis for the identification and formulation of the linearized LPB equation.…”
Section: Introductionmentioning
confidence: 99%