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Related Concept Videos

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...
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...
Applications Of NMR In Biology01:25

Applications Of NMR In Biology

Nuclear magnetic resonance (NMR) spectroscopy is a very valuable analytical technique for researchers. It has been used for more than 50 years as an analytical tool. F. Bloch and E. Purcell formulated NMR in 1946 and won the 1952 Nobel Prize in Physics  for their work. Biological macromolecules such as proteins, nucleic acids, lipids, and organic molecules including pharmaceutical compounds, can be studied using this versatile tool that exploits the magnetic properties of certain nuclei.
The...
Drug Discovery: Overview01:26

Drug 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...
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:
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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NMR-Based Fragment Screening in a Minimum Sample but Maximum Automation Mode
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Published on: June 4, 2021

Ligand based NMR methods for drug discovery.

Christian Ludwig1, Ulrich L Guenther

  • 1HWB-NMR, School of Cancer Sciences, University of Birmingham, Vincent Drive, Edgbaston, Birmingham, B15 2TT, UK.

Frontiers in Bioscience (Landmark Edition)
|March 11, 2009
PubMed
Summary

Ligand-based Nuclear Magnetic Resonance (NMR) methods offer versatile tools for drug discovery. These techniques characterize protein-inhibitor interactions without requiring protein isotopic labeling, aiding hit-to-lead optimization.

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Disentangling Glycan-Protein Interactions: Nuclear Magnetic Resonance (NMR) to the Rescue

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Area of Science:

  • Biochemistry
  • Medicinal Chemistry
  • Structural Biology

Background:

  • Nuclear Magnetic Resonance (NMR) spectroscopy is a well-established technique in drug discovery and lead optimization.
  • NMR offers a unique advantage by integrating structural and functional data to characterize protein-inhibitor interactions.
  • NMR methods are broadly categorized into protein-based and ligand-based experiments.

Purpose of the Study:

  • To highlight the growing importance and application of ligand-based NMR methods in drug discovery.
  • To detail the advantages and specific techniques within ligand-based NMR.
  • To underscore the utility of these methods in screening and lead optimization.

Main Methods:

  • Focus on ligand-based NMR techniques, which do not require isotopic labeling of proteins or ligands.
  • Includes methods such as diffusion experiments, saturation transfer difference (STD-NMR), NOE pumping, waterLOGSY, SALMON, transferred-NOE, and INPHARMA.
  • These methods are broadly applicable and impose minimal constraints on target protein composition.

Main Results:

  • Ligand-based NMR methods provide a wide array of options for determining binding epitopes.
  • These techniques are effective in identifying specific interactions for compounds with relatively low affinity.
  • They offer valuable structural insights without the need for protein crystallization or isotopic labeling.

Conclusions:

  • Ligand-based NMR methods are powerful, versatile tools for drug discovery and hit-to-lead optimization.
  • Their applicability, low-requirement nature, and ability to provide structural information make them highly attractive.
  • These methods enhance the screening and optimization process by detecting weak interactions and offering structural data efficiently.