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Related Concept Videos

Protein-Drug Binding: Determination Methods01:22

Protein-Drug Binding: Determination Methods

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...
The Equilibrium Binding Constant and Binding Strength02:18

The Equilibrium Binding Constant and Binding Strength

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:
The Equilibrium Binding Constant and Binding Strength02:18

The Equilibrium Binding Constant and Binding Strength

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:
Drug Binding to Blood Components01:30

Drug Binding to Blood Components

When drugs enter systemic circulation, they interact with various components of the blood, including proteins such as human serum albumin (HSA), α1-acid glycoprotein (AAG), lipoproteins, globulins, and red blood cells (RBCs).
HSA is the most abundant plasma protein and is vital in drug binding. It contains distinct drug-binding sites, with different drugs exhibiting affinity for specific sites. There are three main drug-binding domains for HSA: sites I, II, and III. These domains are further...
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...
Ligand Binding Sites02:40

Ligand Binding Sites

Proteins are dynamic macromolecules that carry out a wide variety of essential processes; however, the activities of most proteins depend on their interactions with other molecules or ions, known as ligands.
Protein-ligand interactions are quite specific; even though numerous potential ligands surround a cellular protein at any given time, only a particular ligand can bind to that protein. Moreover, a ligand binds only to a dedicated area on the surface of the protein, known as the...

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Related Experiment Video

Updated: Jun 26, 2026

Biosensor-based High Throughput Biopanning and Bioinformatics Analysis Strategy for the Global Validation of Drug-protein Interactions
08:31

Biosensor-based High Throughput Biopanning and Bioinformatics Analysis Strategy for the Global Validation of Drug-protein Interactions

Published on: December 1, 2020

Drug-binding databases.

Luís Fernando Saraiva Macedo Timmers1, Ivani Pauli, Rafael Andrade Caceres

  • 1Faculdade de Biociências, Laboratório de Bioquímica Estrutural, Pontifícia Universidade Católica do Rio Grande do Sul, Porto Alegre, RS, Brazil.

Current Drug Targets
|January 9, 2009
PubMed
Summary
This summary is machine-generated.

Advances in computational power and chemoinformatics have led to numerous online databases for protein-drug interactions. These resources facilitate the identification and acquisition of molecules for virtual screening drug discovery initiatives.

Related Experiment Videos

Last Updated: Jun 26, 2026

Biosensor-based High Throughput Biopanning and Bioinformatics Analysis Strategy for the Global Validation of Drug-protein Interactions
08:31

Biosensor-based High Throughput Biopanning and Bioinformatics Analysis Strategy for the Global Validation of Drug-protein Interactions

Published on: December 1, 2020

Area of Science:

  • Computational chemistry and bioinformatics
  • Drug discovery and development
  • Molecular biology and pharmacology

Background:

  • The internet provides access to vast scientific data, including protein-drug interaction information.
  • Specialized databases are crucial for identifying potential drug candidates for virtual screening.
  • Recent technological advancements have spurred the development of these valuable resources.

Purpose of the Study:

  • To review recent advancements in protein-drug interaction databases.
  • To summarize the applications of these databases in virtual screening projects.
  • To highlight resources for accessing and utilizing potential drug molecules.

Main Methods:

  • Literature review of recent developments in chemoinformatics and database technology.
  • Analysis of existing protein-drug interaction databases.
  • Survey of applications in virtual screening methodologies.

Main Results:

  • Numerous databases for protein-drug interactions have emerged, offering easy access to molecular data.
  • These databases support various stages of drug discovery, from identification to purchase.
  • Key applications in virtual screening initiatives are discussed.

Conclusions:

  • The proliferation of specialized databases significantly aids virtual screening efforts.
  • Accessibility of molecular data through these databases accelerates drug discovery pipelines.
  • Continued development in this area is vital for future pharmaceutical research.