Plegamiento anómalo de proteínas precursoras del Alzheimer a partir del modelo de transición conformacional cuántica

Abstract

Different studies on the progressive neurodegenerative disorder called Alzheimer's disease (AD), reveal that insoluble fibrillar aggregates called amyloids lead to the formation of neuritic plaques that affect memory and all cognitive functions (Lopera, 1999). The sequential action of betasecretase enzymes (BACE) and the gamma-secretase complex on the amyloid precursor protein (APP) trigger the β-amyloid precursor protein from abnormal folding. Previous work carried out by Liaofu Luo has shown from experimental results that protein folding is essentially a quantum transition between conformational states (Luo L. F., 2011). Therefore, it is established that, in an abnormal folding of proteins, the electronic state does not change during the transition process, thus obtaining a general deduction for the abnormal folding energy of the Alzheimer's precursor proteins, which makes it possible to understand its dynamics, and in this way obtain a quantum description of the nature of this disease. Finally, it is expected that the reasoning exposed can be checked in future investigations.