Related Experiment Video
Updated: May 13, 2026
06:26
Nano-Differential Scanning Fluorimetry for Screening in Fragment-based Lead Discovery
Published on: May 16, 2021
Label-free kinetic binding data as a decisive element in drug discovery.
Karl Andersson1, Robert Karlsson, Stefan Löfås
1Biacore AB, Rapsgatan 7 SE-75450 Uppsala, Sweden. stefan.lofas@biacore.com.
Expert Opinion on Drug Discovery
|March 19, 2013
Summary
Drug discovery benefits from label-free kinetic binding data, moving beyond simple affinity. Optimizing association and dissociation rates refines compound selection for better drug-target and drug-ADME interactions.
Area of Science:
- Pharmacology
- Biochemistry
- Drug Discovery
Background:
- Traditional drug discovery often relies on affinity, which can be misleading for drug potency.
- Label-free kinetic binding data offers a more nuanced understanding of drug-target and drug-ADME-marker interactions.
- Emerging technologies enable the acquisition of kinetic data crucial for drug development.
Purpose of the Study:
- To review literature on compound selection in drug discovery, emphasizing kinetic data.
- To highlight the importance of association and dissociation rates in drug-target interactions.
- To explore the role of kinetic profiling in refining drug candidates early in the discovery process.
Main Methods:
- Literature review of studies on kinetic-based binding data in drug discovery.
- Analysis of the significance of association and dissociation rates in drug-protein interactions.
- Examination of how kinetic properties influence compound selection strategies.
Main Results:
- Kinetic data provides valuable insights beyond simple affinity for drug potency.
- Optimizing both association and dissociation rates can yield compounds with improved kinetic profiles.
- Considering kinetic properties of drug-ADME-marker interactions enhances compound quality.
Conclusions:
- Kinetic data on drug-protein interactions is becoming essential in modern drug discovery.
- Understanding and optimizing kinetic parameters are key to successful compound selection.
- Label-free kinetic assays offer a powerful approach to advance drug development.
Related Concept Videos
02:18The 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:
01:22Protein-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...
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...
02:40Ligand 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...
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...
01:16Protein-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,...
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,...
01:26Drug Discovery: Overview
Drug discovery is a multifaceted process involving extensive screening, testing, and optimization of lead compounds to identify potential new drugs for therapeutic use. It combines several approaches, including screening large numbers of natural products, chemical modification of known active molecules, identification of new drug targets, and rational design based on biological mechanisms and drug-receptor structure. These approaches are carried out in both academic research laboratories and...
01:13Physiological Pharmacokinetic Models: Assumption with Protein Binding
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...