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Related Concept Videos

Factors Affecting Protein-Drug Binding: Drug Interactions01:23

Factors Affecting Protein-Drug Binding: Drug Interactions

Drug interactions are a critical aspect of pharmacology and can occur when two or more drugs compete for the same binding site. This competition can result in one drug displacing another, altering the effect of the displaced drug. Drug interactions are complex processes that rely heavily on how much of the displacer drug is present and how strongly it can bind to the same sites as the displaced drug.
Displacement interactions can have varying outcomes, ranging from toxicity to virtually...
Factors Affecting Protein-Drug Binding: Protein-Related Factors01:20

Factors Affecting Protein-Drug Binding: Protein-Related Factors

Drug binding to proteins is a key aspect of pharmacokinetics and can influence a drug's distribution, absorption, and elimination in the body. Several factors, including the drug's physiochemical properties, protein concentration, disease states, and the number of binding sites on the protein, influence this process.
The physicochemical properties of a drug play a significant role in its ability to bind to proteins. Lipophilic drugs, which dissolve in fats, oils, and lipids, can be bound by...
Factors Affecting Protein-Drug Binding: Drug-Related Factors01:18

Factors Affecting Protein-Drug Binding: Drug-Related Factors

Drug binding to proteins is a complex phenomenon influenced by various drug-related factors, each playing a significant role in the interaction between drugs and proteins within the body.
One crucial factor in drug-protein binding is the drug's lipophilicity or its affinity for fat. More lipophilic drugs tend to have higher binding extents. For example, highly lipophilic drugs like cloxacillin exhibit substantial protein binding, with as much as 95% of the drug binding to proteins. In contrast,...
Factors Affecting Protein-Drug Binding: Patient-Related Factors01:29

Factors Affecting Protein-Drug Binding: Patient-Related Factors

Protein-drug binding, a pivotal aspect of pharmacokinetics, is subject to considerable variability influenced by an array of patient-related factors. The intricate interplay of age, individual differences, and pathological conditions significantly impact the binding dynamics and subsequent pharmacological effects.
Age stands as a key determinant in protein-drug binding. Neonates, characterized by low albumin content, experience heightened concentrations of unbound drugs such as phenytoin and...
Drug Distribution: Plasma Protein Binding01:29

Drug Distribution: Plasma Protein Binding

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...
Protein-Drug Binding: Mechanism and Kinetics01:16

Protein-Drug Binding: Mechanism and Kinetics

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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Related Experiment Video

Updated: Jun 25, 2026

Bio-layer Interferometry for Measuring Kinetics of Protein-protein Interactions and Allosteric Ligand Effects
13:57

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

Published on: February 18, 2014

Buffer interference with protein dynamics: a case study on human liver fatty acid binding protein.

Dong Long1, Daiwen Yang

  • 1Department of Biological Sciences, National University of Singapore, Singapore 117543.

Biophysical Journal
|February 17, 2009
PubMed
Summary

Buffer selection is critical for protein studies. This research reveals that MES and Bis-Tris buffers can alter protein dynamics, impacting functional studies and offering insights into ligand binding mechanisms.

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Molecular Spring Constant Analysis by Biomembrane Force Probe Spectroscopy
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Molecular Spring Constant Analysis by Biomembrane Force Probe Spectroscopy

Published on: November 20, 2021

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Last Updated: Jun 25, 2026

Bio-layer Interferometry for Measuring Kinetics of Protein-protein Interactions and Allosteric Ligand Effects
13:57

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

Published on: February 18, 2014

Molecular Spring Constant Analysis by Biomembrane Force Probe Spectroscopy
08:10

Molecular Spring Constant Analysis by Biomembrane Force Probe Spectroscopy

Published on: November 20, 2021

Area of Science:

  • Biochemistry
  • Structural Biology
  • Biophysical Chemistry

Background:

  • Buffer selection is crucial for protein studies using NMR and X-ray crystallography.
  • Previous research suggested minimal impact of MES buffer on protein structures.

Purpose of the Study:

  • To investigate the interaction between MES buffer and human liver fatty acid binding protein (hLFABP).
  • To determine the effect of buffer interaction on protein structure and dynamics.
  • To explore potential implications for protein dynamics studies.

Main Methods:

  • Studied the interaction between MES buffer and hLFABP.
  • Assessed the impact of MES buffer on hLFABP structure and dynamics.
  • Investigated buffer interference using Bis-Tris and fatty acids.

Main Results:

  • Demonstrated a direct, weak interaction between MES and hLFABP.
  • Found that MES significantly affected hLFABP dynamics, not its structure.
  • Observed similar buffer interference with protein dynamics using Bis-Tris.
  • Reported buffer interference with protein dynamics on a microsecond to millisecond timescale.

Conclusions:

  • Buffer interference with protein dynamics is a potential issue in functional studies.
  • This finding provides insights into how hLFABP accommodates ligands.
  • Highlights the importance of considering buffer effects in biophysical studies.