Recent developments in protein–ligand affinity mass spectrometry

✍ Scribed by Niels Jonker; Jeroen Kool; Hubertus Irth; Wilfried M. A. Niessen

• Book ID: 105893846
• Publisher: Springer
• Year: 2010
• Tongue: English
• Weight: 870 KB
• Volume: 399
• Category: Article
• ISSN: 1618-2650
• DOI: 10.1007/s00216-010-4350-z

✦ Synopsis

This review provides an overview of direct and indirect technologies to screen protein–ligand interactions with mass spectrometry. These technologies have as a key feature the selection or affinity purification of ligands in mixtures prior to detection. Specific fields of interest for these technologies are metabolic profiling of bioactive metabolites, natural extract screening, and the screening of libraries for bioactives, such as parallel synthesis libraries and small combichem libraries. The review addresses the principles of each of the methods discussed, with a focus on developments in recent years, and the applicability of the methods to lead generation and development in drug discovery.

FigureSchematic view of the principle of filtration based 96-well affinity selection MS binding assays