Related Experiment Video
Updated: Jan 20, 2026
13:26
Determination of Protein-ligand Interactions Using Differential Scanning Fluorimetry
Published on: September 13, 2014
62.7K
Intrinsic tryptophan fluorescence spectroscopy reliably determines galectin-ligand interactions
Paulina Sindrewicz1, Xiaoxin Li1, Edwin A Yates2
1Department of Cellular and Molecular Physiology, Institute of translational Medicine, University of Liverpool, Liverpool, L69 3GE, UK.
Scientific Reports
|August 16, 2019
Summary
Tryptophan fluorescence spectroscopy (TFS) offers a simple, sensitive method for assessing galectin-ligand interactions, crucial for understanding diseases and developing targeted drugs.
Area of Science:
- Biochemistry
- Molecular Biology
- Glycobiology
Background:
- Galectins regulate diverse physiological and pathological processes, playing key roles in numerous diseases.
- Current methods for assessing galectin-ligand interactions are limited in simplicity and effectiveness.
Purpose of the Study:
- To investigate tryptophan fluorescence spectroscopy (TFS) as a method for quantifying galectin-ligand interactions.
- To evaluate TFS as a potential drug-discovery platform for galectin-targeted therapeutics.
Main Methods:
- Analysis of human galectin members revealed conserved tryptophan residues in carbohydrate-recognition domains.
- Tryptophan fluorescence spectroscopy (TFS) was employed to study interactions between galectins (galectin-2, -3, -4) and various ligands.
- Isothermal titration calorimetry (ITC) was used as a comparative method.
Main Results:
- TFS demonstrated good agreement with ITC measurements for galectin-ligand binding affinities.
- TFS detected weak galectin-ligand interactions that were below the reliable detection limit of ITC.
- TFS validation was confirmed using galectin-3 and a semisynthetic ligand (F3).
Conclusions:
- Tryptophan fluorescence spectroscopy (TFS) is a reliable, sensitive, and simple method for determining galectin-ligand interactions.
- TFS serves as a valuable drug-discovery platform for developing novel galectin-targeted therapeutic agents.
More Related Videos
Related Concept Videos
02:18Intrinsically Disordered Proteins
19.2K
Intrinsically disordered proteins are a group of proteins that do not fold into specific three-dimensional structures. Their structural flexibility allows them to complement ordered proteins to perform functions that are inaccessible to rigid structures. They are more common in eukaryotes than prokaryotes and may either be exclusively intrinsically disordered or hybrid proteins, consisting of a mix of ordered and disordered regions. The absence of a rigid structure in these proteins can be...
19.2K
02:18Intrinsically Disordered Proteins
2.8K
2.8K
02:40Ligand Binding Sites
14.9K
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...
14.9K
01:29Atomic Fluorescence Spectroscopy
919
Atomic fluorescence spectroscopy (AFS) is an analytical technique that involves the electronic transitions of atoms in a flame, furnace, or plasma being excited by electromagnetic (EM) radiation. When these atoms absorb energy, they become excited and subsequently release energy as they return to their original state. This emitted light, or "fluorescence," is observed at a right angle to the incident beam. Both absorption and emission processes transpire at distinct wavelengths, which...
919
01:29Reliability and Validity
13.7K
Reliability and validity are two important considerations that must be made with any type of data collection. Reliability refers to the ability to consistently produce a given result. In the context of psychological research, this would mean that any instruments or tools used to collect data do so in consistent, reproducible ways.
13.7K
01:12Interaction of EM Radiation with Matter: Spectroscopy
3.1K
Electromagnetic (EM) radiation can be considered an oscillating electric and magnetic field propagating through a medium that can interact with matter in its path. The electric field in the radiation can interact with electrical charges in the atoms or molecules in the matter. On the other hand, the magnetic field can interact with the magnetic field in the atomic nucleus. The study of the interaction between electromagnetic radiation and matter is termed spectroscopy. Spectroscopy is the study...
3.1K