β-Lactoglobulin (BLG) binding to highly charged cationic polymer-grafted magnetic nanoparticles: Effect of ionic strength

Qin, Li; Xu, Yisheng; Han, Haoya; Liu, Miaomiao; Chen, Kaimin; Wang, Siyi; Wang, Jie; Xu, Jun; Li, Li; Guo, Xuhong

doi:10.1016/j.jcis.2015.08.056

Cited by 13 publications

(24 citation statements)

References 47 publications

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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%

Interaction of Proteins with Polyelectrolytes: Comparison of Theory to Experiment

et al. 2018

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We discuss recent investigations of the interaction of polyelectrolytes with proteins. In particular, we review our recent studies on the interaction of simple proteins such as human serum albumin (HSA) and lysozyme with linear polyelectrolytes, charged dendrimers, charged networks, and polyelectrolyte brushes. In all cases discussed here, we combined experimental work with molecular dynamics (MD) simulations and mean-field theories. In particular, isothermal titration calorimetry (ITC) has been employed to obtain the respective binding constants K and the Gibbs free energy of binding. MD simulations with explicit counterions but implicit water demonstrate that counterion release is the main driving force for the binding of proteins to strongly charged polyelectrolytes: patches of positive charges located on the surface of the protein become multivalent counterions of the polyelectrolyte, thereby releasing a number of counterions condensed on the polyelectrolyte. The binding Gibbs free energy due to counterion release is predicted to scale with the logarithm of the salt concentration in the system, which is verified by both simulations and experiment. In several cases, namely, for the interaction of proteins with linear polyelectrolytes and highly charged hydrophilic dendrimers, the binding constant could be calculated from simulations to very good approximation. This finding demonstrated that in these cases explicit hydration effects do not contribute to the Gibbs free energy of binding. The Gibbs free energy can also be used to predict the kinetics of protein uptake by microgels for a given system by applying dynamic density functional theory. The entire discussion demonstrates that the direct comparison of theory with experiments can lead to a full understanding of the interaction of proteins with charged polymers. Possible implications for applications, such as drug design, are discussed.

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Section: Introductionmentioning

confidence: 99%

Interaction of Proteins with Polyelectrolytes: Comparison of Theory to Experiment

et al. 2018

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“…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%

Protein–Polyelectrolyte Interaction: Thermodynamic Analysis Based on the Titration Method †

Wang

Zheng

et al. 2019

Polymers

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This review discussed the mechanisms including theories and binding stages concerning the protein–polyelectrolyte (PE) interaction, as well as the applications for both complexation and coacervation states of protein–PE pairs. In particular, this review focused on the applications of titration techniques, that is, turbidimetric titration and isothermal titration calorimetry (ITC), in understanding the protein–PE binding process. To be specific, by providing thermodynamic information such as pHc, pHφ, binding constant, entropy, and enthalpy change, titration techniques could shed light on the binding affinity, binding stoichiometry, and driving force of the protein–PE interaction, which significantly guide the applications by utilization of these interactions. Recent reports concerning interactions between proteins and different types of polyelectrolytes, that is, linear polyelectrolytes and polyelectrolyte modified nanoparticles, are summarized with their binding differences systematically discussed and compared based on the two major titration techniques. We believe this short review could provide valuable insight in the understanding of the structure–property relationship and the design of applied biomedical PE-based systems with optimal performance.

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“…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%

Study of Interactions between Antigens and Polymeric Adjuvants in Vaccines by Frontal Analysis Continuous Capillary Electrophoresis

et al. 2020

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Vaccine adjuvants are used to enhance the immune response induced by antigens that have insufficient immunostimulatory capabilities. The present work aims at developing frontal analysis continuous capillary electrophoresis (FACCE) methodology for the study of antigenadjuvant interactions in vaccine products. After method optimization using three cationic model proteins, namely lysozyme, cytochrome C and ribonuclease A, FACCE was successfully implemented to quantify the free antigen and thus to determine the interaction parameters (stoichiometry and binding constant) between an anionic polymeric adjuvant (polyacrylic acid, SPA09), and a cationic vaccine antigen in development for the treatment of Staphylococcus aureus. The influence of the ionic strength of the medium on the interactions was investigated. A strong dependence of the binding parameters with the ionic strength was observed. The concentration of the polymeric adjuvant was also found to significantly modify the ionic strength of the formulation, the extent of which could be estimated and corrected.

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β-Lactoglobulin (BLG) binding to highly charged cationic polymer-grafted magnetic nanoparticles: Effect of ionic strength

Cited by 13 publications

References 47 publications

Interaction of Proteins with Polyelectrolytes: Comparison of Theory to Experiment

Interaction of Proteins with Polyelectrolytes: Comparison of Theory to Experiment

Protein–Polyelectrolyte Interaction: Thermodynamic Analysis Based on the Titration Method †

Study of Interactions between Antigens and Polymeric Adjuvants in Vaccines by Frontal Analysis Continuous Capillary Electrophoresis

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