Intrinsically disordered proteins (IDPs) are polypeptides containing long regions (more than 30 consecutive residues) that lack stable secondary structures (α-helix and β-strand). Bioinformatics analyses of several proteomes indicate that more than one third of eukaryotic proteins are intrinsically disordered. Many of them are involved in signalling pathways or regulation processes, and are considered as critical hubs in protein interaction networks (Uversky 2011). Overexpressions, mutations or dysfunctions of these proteins are involved in many human diseases, including cancer, diabetes, cardiovascular and neurodegenerative disorders (Uversky et al. 2009). Thus, a very promising route for the development of new drugs against these diseases was to develop drugs that could interfere with the protein-protein interactions involving IDPs. (Copied from article).