Recent developments in protein–ligand affinity mass spectrometry

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

Studying protein–protein affinity and immobilized ligand–protein affinity interactions using MS-based methods

This review discusses the most important current methods employing mass spectrometry (MS) analysis for the study of protein affinity interactions. The methods are discussed in depth with particular reference to MS-based approaches for analyzing protein–protein and protein–immobilized ligand interactions, analyzed either directly or indirectly. First, we introduce MS methods for the study of intact protein complexes in the gas phase. Next, pull-down methods for affinity-based analysis of protein–protein and protein–immobilized ligand interactions are discussed. Presently, this field of research is often called interactomics or interaction proteomics. A slightly different approach that will be discussed, chemical proteomics, allows one to analyze selectivity profiles of ligands for multiple drug targets and off-targets. Additionally, of particular interest is the use of surface plasmon resonance technologies coupled with MS for the study of protein interactions. The review addresses the principle of each of the methods with a focus on recent developments and the applicability to lead compound generation in drug discovery as well as the elucidation of protein interactions involved in cellular processes. The review focuses on the analysis of bioaffinity interactions of proteins with other proteins and with ligands, where the proteins are considered as the bioactives analyzed by MS

Niobium Coatings for the HIE-ISOLDE QWR Superconducting Accelerating Cavities

The HIE-ISOLDE (High Intensity and Energy at ISOLDE) project is the upgrade of the existing ISOLDE (Isotope Separator On Line DEvice) facility at CERN, which is dedicated to the production of a large variety of radioactive ion beams for nuclear physics experiments. A new linear accelerator made of 20 ȕ=10.3% and 12 ȕ=6.3% quarter-wave resonators (QWR) superconducting (SC) accelerating cavities at 101 MHz will be built, and in a first phase two cryomodules of 5 high-ȕ cavities each are scheduled to accelerate first beams in 2015. The cavities are made of a copper substrate, with a sputter-coated superconductive niobium (Nb) layer, operated at 4.5 K with an accelerating field of 6 MV/m at 10W Radio-Frequency (RF) losses (Q=4.5· 108). In this paper we will discuss the baseline surface treatment and coating procedure which allows obtaining the required performance, as well as the steps undertaken in order to prepare series production of the required number of cavities guaranteeing their quality and functionality