TY - JOUR T1 - Binding Profile Mapping of the S100 Protein Family Using a High-throughput Local Surface Mimetic Holdup Assay JF - bioRxiv DO - 10.1101/2020.12.02.407676 SP - 2020.12.02.407676 AU - Márton A. Simon AU - Éva Bartus AU - Beáta Mag AU - Eszter Boros AU - Lea Roszjár AU - Gergő Gógl AU - Gilles Travé AU - Tamás A. Martinek AU - László Nyitray Y1 - 2020/01/01 UR - http://biorxiv.org/content/early/2020/12/02/2020.12.02.407676.abstract N2 - S100 proteins are small, typically homodimeric, vertebrate-specific EF-hand proteins that establish Ca2+-dependent protein-protein interactions in the intra- and extracellular environment and are overexpressed in various pathologies. There are about 20 distinct human S100 proteins with numerous potential partner proteins. Here, we used a quantitative holdup assay to measure affinity profiles of most members of the S100 protein family against a library of chemically synthetized foldamers. The profiles allowed us to quantitatively map the binding promiscuity of each member towards the foldamer library. Since the library was designed to systematically contain most binary natural amino acid side chain combinations, the data also provide insight into the promiscuity of each S100 protein towards all potential naturally-occurring S100 partners in the human proteome. Such information will be precious for future drug design of modulators of S100 pathological activities.Competing Interest StatementThe authors have declared no competing interest.AUCarea under curveFPfluorescence polarizationHTPhigh-throughputLC-MSliquid chromatography - mass spectrometryHUholdupPPIprotein-protein interactionsRP-HPLCreverse phased high performance liquid chromatographySDS-PAGEsodium dodecyl sulfate polyacrylamide gel electrophoresis ER -