相关实验视频

Updated: Jun 28, 2025

A Rapid and Quantitative Fluorimetric Method for Protein-Targeting Small Molecule Drug Screening
08:34

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

Published on: October 16, 2015

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使用多光谱和分子对接技术,了解巴斯皮龙与人血清白蛋白的结合

Javad Sargolzaei1, Elaheh Jalali1, Parisa Rajabi2

  • 1Department of Biology, Faculty of Science, Arak University, Arak, 38156-8-8349, Iran.

Heliyon
|April 19, 2024
PubMed
概括

这项研究表明,巴斯皮龙通过疏水性相互作用与人血清白蛋白 (HSA) 结合,证实了HSA.

关键词:
布斯皮龙 (buspirone) 是一种可靠的药物.在平衡透析中进行透析.人类血清专素的人类血清专素分子对接是分子对接.频谱学是一种光谱学.

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Biosensor-based High Throughput Biopanning and Bioinformatics Analysis Strategy for the Global Validation of Drug-protein Interactions08:31

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Published on: December 1, 2020

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Thermostabilization, Expression, Purification, and Crystallization of the Human Serotonin Transporter Bound to S-citalopram12:21

Thermostabilization, Expression, Purification, and Crystallization of the Human Serotonin Transporter Bound to S-citalopram

Published on: November 27, 2016

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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...
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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...
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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...
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Anxiolytic Drugs: Benzodiazepines and Buspirone01:29

Anxiolytic Drugs: Benzodiazepines and Buspirone

Benzodiazepines are a class of anxiolytic drugs known for their rapid efficacy and high therapeutic-to-lethal dose ratio, but with a potential risk of drug dependence. These drugs are lipophilic, allowing for rapid absorption after oral administration, eventually reaching the central nervous system (CNS). Once in the CNS, benzodiazepines bind to the allosteric site of the GABAA receptor. This binding enhances the inhibitory effects of the neurotransmitter GABA. By doing so, they prevent...
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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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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:
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