RT Journal Article SR Electronic T1 Binding Profile Mapping of the S100 Protein Family Using a High-throughput Local Surface Mimetic Holdup Assay JF bioRxiv FD Cold Spring Harbor Laboratory SP 2020.12.02.407676 DO 10.1101/2020.12.02.407676 A1 Márton A. Simon A1 Éva Bartus A1 Beáta Mag A1 Eszter Boros A1 Lea Roszjár A1 Gergő Gógl A1 Gilles Travé A1 Tamás A. Martinek A1 László Nyitray YR 2020 UL http://biorxiv.org/content/early/2020/12/02/2020.12.02.407676.abstract AB 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