Fiche publication
Date publication
avril 2022
Journal
Scientific reports
Auteurs
Membres identifiés du Cancéropôle Est :
Dr TRAVE Gilles
,
Dr GOGL Gergo
Tous les auteurs :
Simon MA, Bartus É, Mag B, Boros E, Roszjár L, Gógl G, Travé G, Martinek TA, Nyitray L
Lien Pubmed
Résumé
S100 proteins are small, typically homodimeric, vertebrate-specific EF-hand proteins that establish Ca-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 to interfere with S100 related pathologies.
Référence
Sci Rep. 2022 Apr 7;12(1):5904
