ABSTRACT
Alzheimer's disease (AD) is a progressive neurodegenerative disorder of the brain that leads to dementia. According to the amyloid hypothesis, abnormal aggregation of amyloid-ß (Aß) in the brain triggers tau aggregation, microglial activation, synaptic dysfunction, and neuronal loss, ultimately resulting in cognitive decline. Transgenic animals exhibiting well-established AD-like pathology have been variable while testing the effects of Aß immunotherapy. The humanized version of the m266 IgG1 mAb that binds the central region of Aß and has more affinity to monomers than to soluble and toxic species in patients with mild AD is Solanezumab. The cross-reactivity and the inflammatory alterations observed in some patients, along with the efficiency of mAb to cross the blood–brain barrier regarding passive immunization, have to be improved. Immunization for decreasing amyloid pathology and improving cognitive function effectiveness does not depend on the titer. Independent of the specific amino acid sequence, it is now concluded that the critical epitope is a pathology-specific confirmation of the peptide backbone.
