Generic placeholder image

Current Pharmaceutical Biotechnology


ISSN (Print): 1389-2010
ISSN (Online): 1873-4316

Ligand-Receptor Interactions in Live Cells by Fluorescence Correlation Spectroscopy

Author(s): Aladdin Pramanik

Volume 5, Issue 2, 2004

Page: [205 - 212] Pages: 8

DOI: 10.2174/1389201043377002

Price: $65


Receptor binding studies most often require the use of radioactively labeled ligands. In certain cases, the numbers of receptors are few per cell and no specific binding is detected because of a high background. Specific interactions between certain ligands (e.g. peptides, hormones, natural products) and their receptors are, therefore, often overlooked by the conventional binding technique. Fluorescence correlation spectroscopy (FCS) allows detection of the interaction of ligands with receptors in their native environment in live cells in a tiny confocal volume element (0.2 fl) at single-molecule detection sensitivity. This technique permits the identification of receptors which were not possible before to detect by isotope labeling. The beauty of the FCS technique is that there is no need for separating an unbound ligand from a bound one to calculate the receptor bound and free ligand fractions. This review will show FCS as a sensitive and a rapid technique to study ligand-receptor interaction in live cells and will demonstrate that the FCS-analysis of ligand-receptor interactions in live cells fulfils all the criteria of a ligand binding to its receptor i.e. it is able to provide information on the affinity and specificity of a ligand, binding constant, association and dissociation rate constants as well as the number and mobility of receptors carrying a fluorescently labeled ligand. This review is of pharmaceutical significance since it will provide insights on how FCS can be used as a rapid technique for studying ligand-receptor interactions in cell cultures, which is one step forward towards a high throughput drug screening in cell cultures.

Keywords: fluorescence, brownian motion, ligand, receptor

Rights & Permissions Print Cite
© 2024 Bentham Science Publishers | Privacy Policy