Abstract

Causative agents of Alzheimer’s disease are 1) amyloid β foldings, 2) neurofibrillary tangles, and 3) reactive gliosis. Interaction of Aβ with the prion protein within neurons has recently been suggested to be the basis for drug discovery. Prion protein is a membrane protein found on cell surfaces of diverse types [1]. The accumulation of misfolded and unfolded proteins (UP) generates stress in the endoplasmic reticulum. This stress worsens the health of the regular function of neuronal cells. The role of unfolded protein response in T cell development and function has also been acknowledged [2]. The induction of Femto particles (Fps) is proposed inside G protein-coupled receptors at an appropriate point in time to monitor the accumulation of unfolded proteins and to control the misfolding of amyloid β. These new particles of 10-15m are proposed to be produced in neurons of the bloodbrain barrier (BBB). Protons released by hemoglobin can be glued to their antiparticle, i.e., antiproton, in the conformational space of partially folded amyloid β polypeptides. Portable Penning antiproton traps are now available at CERN. Gluing of protons and antiprotons to form a femto particle is mediated by dopamine, a neurotransmitter in the excitatory synapses.

Intraneuronal oxygen homeostasis also contributes to the control of the progression of the disease. Quantum entanglement between two fps (cf. Fig. 8), one in the neurons of the neurovascular system (NVU) and the other in cerebrospinal fluid (CSF), may be used to assess the efficiency of the process in a patient with AD. Our approach to the discovery of a drug for AD is based on monitoring and controlling the misfolding of amyloid β and the initiation of folding of unfolded proteins by the intervention of femto particles.