Related Experiment Video

Updated: Dec 24, 2025

Luminophore Formation in Various Conformations of Bovine Serum Albumin by Binding of GoldIII
08:26

Luminophore Formation in Various Conformations of Bovine Serum Albumin by Binding of GoldIII

Published on: August 31, 2018

7.2K

Binding of a Fatty Acid-Functionalized Anderson-Type Polyoxometalate to Human Serum Albumin

Aleksandar Bijelic1, Anatolie Dobrov1, Alexander Roller2

  • 1Fakultät für Chemie, Institut für Biophysikalische Chemie, Universität Wien, Althanstraße 14, 1090 Wien, Austria.

Inorganic Chemistry
|April 8, 2020
PubMed

More Related Videos

Preparation of Polypentafluorophenyl acrylate Functionalized SiO2 Beads for Protein Purification08:51

Preparation of Polypentafluorophenyl acrylate Functionalized SiO2 Beads for Protein Purification

Published on: November 19, 2018

10.1K
A Rapid and Quantitative Fluorimetric Method for Protein-Targeting Small Molecule Drug Screening08:34

A Rapid and Quantitative Fluorimetric Method for Protein-Targeting Small Molecule Drug Screening

Published on: October 16, 2015

10.4K

Related Concept Videos

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...
8.1K
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...
433
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...
455
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...
400
Complexometric Titration: Ligands00:43

Complexometric Titration: Ligands

Different monodentate and polydentate ligands are used as complexing agents in complexometric titration reactions. The formation of complexes by mono- and bidentate ligands involves two or more intermediate steps, limiting their use as complexing agents. In comparison, polydentate ligands can form complexes with metal ions in a single-step process, facilitating sharper end points. This means polydentate ligands, such as amino carboxylic acid derivatives, are most commonly employed in...
2.1K