Although post-translational modifications (PTMs) such as phosphorylation, ubiquitination, nitration, and truncation have been implicated in modulating the process of protein aggregation and related toxicity, most screening assays and drug development programs today are still based on using unmodified proteins or platforms that do not capture the true biochemical properties of related proteins. This was mostly due to the lack of enabling technologies and platforms.

Based on 15 years of R&D at the EPFL, ND Biosciences is now capable of introducing site-specific PTMs at any position along the sequence of proteins implicated in NDs. This allows the recapitulation of both the biochemical and structural properties of these proteins, and the generation of libraries of proteins bearing either single or multiple PTMs, but also in the context of relevant protein conformations. Importantly, these technologies have been successfully applied for the modification and large scale production of libraries of several ND-causing proteins including α-Synuclein, Tau, Huntingtin and TDP43, which are key players in the pathogenesis PD, AD, Huntington’s disease and Amyotrophic lateral sclerosis, respectively. These libraries are utilized by ND Biosciences for the development, identification and profiling of novel binders with therapeutic potential, and for the development of sensitive and accurate diagnostic assays and imaging agents that capture the diversity of pathologically relevant species in different diseases.