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Related Concept Videos

The Equilibrium Binding Constant and Binding Strength02:18

The Equilibrium Binding Constant and Binding Strength

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The equilibrium binding constant (Kb) quantifies the strength of a protein-ligand interaction. Kb can be calculated as follows when the reaction is at equilibrium:
15.1K
The Equilibrium Binding Constant and Binding Strength02:18

The Equilibrium Binding Constant and Binding Strength

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Ionic Strength: Overview01:12

Ionic Strength: Overview

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The ionic strength of a solution is a quantitative way of expressing the total electrolyte concentration of a solution. This concept was first introduced in 1921 by two American physical chemists, Gilbert N. Lewis and Merle Randall, while describing the activity coefficient of strong electrolytes. During the calculation of ionic strength (I or μ), all the cations and anions are considered. However, the concentration (c) of an ion with a greater charge number (z) has a greater contribution...
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Ionic Strength: Effects on Chemical Equilibria01:19

Ionic Strength: Effects on Chemical Equilibria

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The addition of an inert ionic compound increases the solubility of a sparingly soluble salt. For example, adding potassium nitrate to a saturated solution of calcium sulfate significantly enhances the solubility of calcium sulfate. Le Châtelier's principle cannot predict this shift in the equilibrium. Instead, this could be explained in terms of changes in the effective concentration of the ions in solution in the presence of added inert salt.
In this solution, the primary...
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Ionic Bonds00:42

Ionic Bonds

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Overview
When atoms gain or lose electrons to achieve a more stable electron configuration they form ions. Ionic bonds are electrostatic attractions between ions with opposite charges. Ionic compounds are rigid and brittle when solid and may dissociate into their constituent ions in water. Covalent compounds, by contrast, remain intact unless a chemical reaction breaks them.
Opposing Charges Hold Ions Together in Ionic Compounds
Ionic bonds are reversible electrostatic interactions between ions...
131.4K
Molecular and Ionic Solids02:54

Molecular and Ionic Solids

20.2K
Crystalline solids are divided into four types: molecular, ionic, metallic, and covalent network based on the type of constituent units and their interparticle interactions.
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Updated: Feb 8, 2026

Synthesis of Bimetallic Pt/Sn-based Nanoparticles in Ionic Liquids
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Ionic Strength-Responsive Binding between Nanoparticles and Proteins.

Xiaohan Wang1, Shi Zhang1, Yisheng Xu1,2,3

  • 1State Key Laboratory of Chemical Engineering , East China University of Science and Technology , 200237 Shanghai , P. R. China.

Langmuir : the ACS Journal of Surfaces and Colloids
|June 24, 2018
PubMed
Summary
This summary is machine-generated.

Hydrophobic interactions on protein-nanoparticle binding are crucial. Optimizing magnetic nanoparticle (MNP) surface hydrophobicity and ionic strength tunes binding affinity for selective separation and delivery systems.

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Area of Science:

  • Biomaterials Science
  • Surface Chemistry
  • Nanotechnology

Background:

  • Electrostatic interactions dominate protein-nanoparticle (NP) binding studies.
  • The role of hydrophobic interactions in protein-NP binding, especially with charged NPs, is understudied.
  • Globular proteins possess abundant hydrophobic residues that can influence binding.

Purpose of the Study:

  • To investigate the influence of surface hydrophobicity on the binding of proteins to charged magnetic nanoparticles (MNPs).
  • To explore the combined effects of ionic strength and hydrophobicity on MNP-protein interactions.
  • To develop a tunable system for selective separation and delivery applications.

Main Methods:

  • Preparation of positively charged MNPs using atom transfer radical polymerization.
  • Surface hydrophobicity differentiation via postpolymerization quaternization.
  • Qualitative and quantitative analysis of MNP-β-lactoglobulin (BLG) binding using turbidimetric titration, dynamic light scattering, and isothermal titration calorimetry.

Main Results:

  • Binding affinity showed a shift with increasing ionic strength based on MNP surface hydrophobicity.
  • Higher surface hydrophobicity led to weaker binding at low ionic strength but stronger binding at high ionic strength.
  • This behavior is attributed to differential ionic strength responsiveness of hydrophobic and electrostatic interactions.

Conclusions:

  • Optimizing MNP surface hydrophobicity and ionic strength allows for fine-tuning of binding affinity.
  • The developed system demonstrates significant potential for creating highly selective and efficient separation and delivery systems.
  • Understanding hydrophobic interactions is key to designing advanced nanomaterial-based biological applications.