Modern mass spectrometry is able to extract much more information from biological samples than just the molecular weight. While in conventional mass spectrometry all information of non-covalent interaction is lost, in native mass spectrometry protein-protein or protein-ligand interactions are retained in the gas phase. NUVISAN offers native mass spectrometry as an addition to our biophysics platform for analysis of protein complexes consisting of other proteins, SMOLs or co-factors to determine stoichiometries and binding affinities.
Beside classic light-based detection technologies for high-throughput screening of small molecule libraries, NUVISAN also offers a mass spectrometry-based automated, label-free, direct-detection approach: RapidFire-MS - an electrospray-based technology in 384‐well plate format which can cope with complex enzyme preparations and salt contaminations. For even higher throughput in 1536-well plate format state-of-the-art matrix‐assisted laser desorption/ionization time‐of‐flight (MALDI‐ToF) MS can be used.
Targeted metabolomics allows the relative or absolute quantification of a predefined set of endogenous metabolites. NUVISAN offers targeted metabolite analysis of different matrices, as cell culture samples, plasma, and tissue samples. Targeted metabolomics provides, among others, information on cellular target engagement and the pharmacodynamics of cellular metabolite levels induced by drug treatments.
Beside classical technologies as eg. analytical SEC, nanoDSF and SLS we offer mass spectrometry to identify and characterize proteins. We analyze the homogeneity of protein preparations, investigate posttranslational modification of proteins, and can provide information on co-factor binding of proteins via native mass spectrometry.
Covalent binders have long been considered adventurous but have now regained widespread attention in drug discovery. Denaturing mass spectrometry by LC-ESI-MS or MALDI-MS turned out to be the gold standard to screen small covalent libraries or to study covalent binders by determine their kinact/KI values.
Proteomics enables the global and targeted analysis of proteins, including protein identification from purified proteins and complex protein samples, quantification based on label-free and isotope labeling (SILAC and TMT) techniques, detection and localization of posttranslational modifications (PTMs).