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23rd Human Proteome Organization World Congress

In proteomic assays such as the SomaScan® Assay, thousands of affinity reagents are utilized simultaneously to achieve comprehensive profiling. This presentation introduces an innovative methodology to evaluate the specificity of these binders. For this study native cellular proteins were separated into 140 fractions, categorized by subcellular location and size. These fractions underwent parallel analysis using mass spectrometry (MS) and the SomaScan Assay, generating intricate chromatograms. The specificity of SOMAmer® Reagents was determined by correlating their binding patterns with the MS data. Additionally, by employing orthogonal separation techniques such as ion exchange chromatography (IEX), we aim to establish distinct profiles for each target protein. We will also present cases where this method is integrated with immunoprecipitation and MS for the direct identification of bound proteins.Speaker Bio:&nbsp;Fridtjof Lund-Johansen is a principal investigator at Oslo University Hospital. His research focus is the interface between affinity- and mass spectrometry based proteomics. Among his inventions is a technology known as Microsphere Affinity Proteomics, which is analogous to a highly multiplexed western blot and MAP protein arrays, useful for highly multiplexed virus serology and detection of targets for autoantibodies. Currently, the MAP platform is adapted to allow library-on-library screens to train machine learning algorithms to predict antibody antigen interactions.