2015
DOI: 10.1016/j.jcis.2015.08.056
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β-Lactoglobulin (BLG) binding to highly charged cationic polymer-grafted magnetic nanoparticles: Effect of ionic strength

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Cited by 13 publications
(24 citation statements)
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“…45,46 The polyelectrolyte chains and brushes thus obtained interact strongly with proteins in aqueous solution and form a variety of protein-polyelectrolyte assemblies. 3,[47][48][49][50] Such systems are of general importance in nanotechnology since polymer chains are often used to prevent the adsorption of proteins onto nanoparticles. 51 Proteins that adsorb to nanoparticles, e.g., in the blood stream may denaturate and thus trigger an immune response of the body.…”
Section: Introductionmentioning
confidence: 99%
“…45,46 The polyelectrolyte chains and brushes thus obtained interact strongly with proteins in aqueous solution and form a variety of protein-polyelectrolyte assemblies. 3,[47][48][49][50] Such systems are of general importance in nanotechnology since polymer chains are often used to prevent the adsorption of proteins onto nanoparticles. 51 Proteins that adsorb to nanoparticles, e.g., in the blood stream may denaturate and thus trigger an immune response of the body.…”
Section: Introductionmentioning
confidence: 99%
“…Moreover, the PE chains grafted to nanoparticles are more rigid and less flexible than its free counterparts in aqueous solution, so spatial constraints mutually exerted by both nanoparticles and proteins have to be considered in addition to the interplay between different surface functionalities. For example, positive PE-modified magnetic nanoparticles were prepared and their binding affinity toward proteins, characterized by turbidimetric titration and ITC, was enhanced at higher ionic strengths because of their closer inter-particle distance caused by screened mutual repulsion (Figure 6) [34]. The calculated surface potential of proteins conformed well to the binding constant derived from ITC, providing convincing evidence for the proposed mechanism.…”
Section: Thermodynamic Studies Of the Protein–pe Interactionmentioning
confidence: 79%
“…When protein–PE complexation occurs, charge patches with the same and opposite charges both interact with PEs, generating a short-range attraction/long range repulsion (SALR) effect [31]. Therefore, an appropriate amount of salt could always screen long-range repulsions, but preserve short-range attractions, leading to maximal binding affinity at certain ionic strength, and the non-monotonic ionic dependence is commonly observed in many cases for both linear PEs and PE-functionalized nanoparticles [32,33,34]. Moreover, charge patches profiles of proteins with similar p I or even structures could be evidently different, such that their phase boundaries of complexation and coacervation/precipitation could diverge with regard to each other.…”
Section: Understanding Of Protein–pe Binding Mechanismsmentioning
confidence: 99%
“…A strong dependence of protein/polyelectrolyte interactions with the ionic strength has been reported in the literature [75][76][77] . To study the impact of the ionic strength on the interaction, five buffers were prepared at pH 7.4, with different ionic strengths ranging from 118 to 268 mM.…”
Section: Impact Of the Ionic Strength On Antigen-adjuvant Interactionsmentioning
confidence: 89%