AmyPore history

AmyPore builds on the research work of two internationally recognised academic researchers, Professors of Biochemistry & Molecular Biology at Aix-Marseille University: Prof. Jacques Fantini and Prof. Nouara Yahi.

After more than 10 years of research into the infection and resistance mechanisms of the AIDS virus, in 2002 they decided to tackle a new problem: understanding the molecular causes of Alzheimer’s disease and Parkinson’s disease. At the time, the scientific community was focusing on the protein aggregates that accumulate in the brain, in the form of amyloid plaques (Alzheimer’s) or Lewy bodies (Parkinson’s). These aggregates contain particular proteins known as “amyloid proteins”: the β-amyloid peptide (Aβ) for Alzheimer’s, α-synuclein for Parkinson’s.

However, the guilt of these aggregates runs up against the observation that amyloid plaques can be present in the brains of healthy individuals, at levels as high as in patients suffering from Alzheimer’s disease [1–3]. In fact, the presence of amyloid plaques does not, in itself, cause cognitive damage.  

J. Fantini and N. Yahi therefore set this avenue aside to turn to smaller structures, known as “oligomers”, also formed by the Aβ and α-synuclein proteins. Several studies have shown that the severity of symptoms correlates with neither the quantity nor the size of the plaques, whereas it is proportional to the amounts of oligomers in the brain [4,5]. Developing new strategies targeting the oligomers was therefore, from the very start of J. Fantini and N. Yahi’s work, a therapeutic priority for Alzheimer’s and Parkinson’s diseases. It was with this objective that they carried out their research into the mechanisms by which amyloid protein oligomers form [6–9].

J. Fantini and N. Yahi have deciphered the biological code that allows amyloid proteins to bind to brain cells, the step preceding the formation of amyloid pores. They thereby demonstrated that these proteins behave as neurotoxins that must be neutralised in order to cure these diseases. They chose to target a particular category of molecules, the gangliosides, which, following the instructions of the biological code they elucidated, allow amyloid proteins to bind to brain cells and to generate neurotoxic oligomers.

Years ahead of their international competitors [10], J. Fantini and N. Yahi drew on their fundamental discovery to create, with the help of artificial intelligence, a molecule with a greater affinity for brain cells than the amyloid proteins themselves [9]. This molecule offers an innovative approach to the treatment of Alzheimer’s and Parkinson’s diseases [11–13]. It is the therapeutic peptide AmyP53 developed by the company AmyPore.