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Related Concept Videos

Protein-Drug Binding: Determination Methods01:22

Protein-Drug Binding: Determination Methods

694
Determining protein-drug binding can be achieved through indirect and direct methods, each providing valuable insights into the interaction between proteins and drugs.
Indirect methods involve isolating the bound drug from its free form in biological samples such as blood, serum, or plasma. These techniques aim to measure the percentage of drugs bound to proteins. Equilibrium dialysis is a commonly used method where the free drug concentration at equilibrium is measured by separating the bound...
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Protein-Drug Binding: Mechanism and Kinetics01:16

Protein-Drug Binding: Mechanism and Kinetics

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Protein-drug binding refers to the interaction between drugs and proteins within the body. This binding process can occur intracellularly, involving drug interactions with enzymes or receptors within cells, or extracellularly, involving plasma proteins in the blood.
Various forces drive these interactions, including hydrogen bonds, hydrophobic interactions, ionic bonds, electrostatic interactions, and van der Waals forces. These bonds enable drugs to bind to specific sites on proteins,...
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Physiological Pharmacokinetic Models: Assumption with Protein Binding01:13

Physiological Pharmacokinetic Models: Assumption with Protein Binding

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Physiological models with protein binding in pharmacokinetics offer a sophisticated approach to understanding drug disposition. These models consider drug-protein interactions, enabling them to effectively predict drug concentrations in different organs and tissues. This precision aids in accurate drug dosing, providing a significant advantage over conventional models. A key process within these models is equilibration, which ensures that drug concentrations achieve a steady state within the...
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Drug Distribution: Plasma Protein Binding01:29

Drug Distribution: Plasma Protein Binding

9.5K
Drugs predominantly attach to plasma proteins, with only a small percentage remaining unbound. The unbound portion can be calculated as one minus the bound fraction. Acidic drugs form large, inactive complexes by reversibly binding to plasma albumin, which prevents them from diffusing across biological barriers. These drug-protein complexes act as reservoirs for the drugs. As the concentration of unbound drugs decreases, these complexes quickly dissociate to release the free drug, maintaining...
9.5K
Nonlinear Pharmacokinetics: Bioavailability and Protein-Drug Binding01:22

Nonlinear Pharmacokinetics: Bioavailability and Protein-Drug Binding

662
When a drug follows nonlinear pharmacokinetics, its bioavailability, the amount of the drug that reaches the systemic circulation, can change with different doses. This is due to the presence of a saturable pathway. The pathway becomes saturated as the drug concentration increases, decreasing the absorption rate. Consequently, the drug's bioavailability may be lower than expected at higher doses.
To quantify the extent of bioavailability, pharmacologists often use a parameter called .
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The Equilibrium Binding Constant and Binding Strength02:18

The Equilibrium Binding Constant and Binding Strength

15.3K
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:
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Determination of High-affinity Antibody-antigen Binding Kinetics Using Four Biosensor Platforms
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Protein Binding Kinetics in Multimodal Systems: Implications for Protein Separations.

Kartik Srinivasan1, Mirco Sorci1, Lars Sejergaard1

  • 1Howard P. Isermann Department of Chemical and Biological Engineering and Center for Biotechnology and Interdisciplinary Studies, Rensselaer Polytechnic Institute , Troy, New York 12180, United States.

Analytical Chemistry
|December 8, 2017
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Summary

Understanding protein interactions with multimodal ligands is key for chromatography. This study used quartz crystal microbalance with dissipation (QCM-D) to reveal how ligand accessibility and mobile phase modifiers impact protein adsorption and desorption kinetics.

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Bio-layer Interferometry for Measuring Kinetics of Protein-protein Interactions and Allosteric Ligand Effects
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Area of Science:

  • Biophysical Chemistry
  • Chromatography Science
  • Surface Science

Background:

  • Multimodal (MM) chromatography utilizes ligands with multiple interaction sites.
  • Protein binding kinetics are crucial for chromatographic selectivity but are complex.
  • Understanding these kinetics requires well-defined model systems.

Purpose of the Study:

  • To investigate the kinetic processes of protein interaction with self-assembled monolayers (SAMs) of multimodal ligands.
  • To determine the impact of ligand accessibility and mobile phase modifiers (arginine, guanidine) on protein adsorption and desorption kinetics.
  • To correlate kinetic data with chromatographic retention behavior.

Main Methods:

  • Fabrication of SAMs mimicking chromatographic multimodal resins with varying aromatic moiety accessibility.
  • Utilizing quartz crystal microbalance with dissipation (QCM-D) to monitor kinetic processes.
  • Determining kinetic parameters for protein adsorption and desorption.
  • Comparing kinetic data with chromatographic retention data.

Main Results:

  • Ligand aromatic moiety accessibility significantly influences protein adsorption/desorption kinetics and chromatographic retention.
  • Arginine and guanidine exhibit distinct effects on protein kinetics; arginine decreased adsorption and increased desorption for cytochrome C, while guanidine increased desorption.
  • Guanidine increased adsorption and moderately increased desorption for α-chymotrypsin, explaining increased salt elution concentration.
  • Two distinct kinetic scenarios were observed for cytochrome C with varying arginine concentrations.

Conclusions:

  • Protein adsorption kinetics, influenced by mobile phase modifiers and ligand chemistry, are critical for achieving selectivity in multimodal chromatography.
  • The accessibility of aromatic moieties in MM ligands plays a vital role in modulating protein-ligand interactions.
  • QCM-D provides valuable insights into the dynamic processes governing protein behavior in chromatographic systems.