Diversity of amyloid beta peptide actions

Abstract

Abstract Fibril formation by amyloidogenic proteins and peptides is considered the cause of a number of incurable diseases. One of the most known amyloid diseases is Alzheimer’s disease (AD). Traditionally, amyloidogenic beta peptides Aβ40 and Aβ42 (Aβs) are considered as main causes of AD and the foremost targets in AD fight. The main efforts in pharmacology are aimed at reducing Aβs concentration to prevent their accumulation, aggregation, formation of senile plaques, neuronal death, and neurodegeneration. However, a number of publications have demonstrated certain beneficial physiological effects of Aβs. Simultaneously, it is indicated that the effects of Aβs turn into pathological due to the development of certain diseases in the body. The accumulation of C- and N-terminal truncated Aβs under diverse conditions is supposed to play a role in AD development. The significance of transformation of glutamate residue at positions 3 or 11 of Aβs catalyzed by glutaminyl cyclase making them more degradation resistant, hydrophobic, and prone to aggregation, as well as the participation of dipeptidyl peptidase IV in these transformations are discussed. The experimental data presented confirm the maintenance of physiological, nonaggregated state of Aβs by plant preparations. In conclusion, this review suggests that in the fight against AD, instead of removing Aβs, preference should be given to the treatment of common diseases. Glutaminyl cyclase and dipeptidyl peptidase IV can be considered as targets in AD treatment. Flavonoids and plant preparations that possess antiamyloidogenic propensity are proposed as beneficial neuroprotective, anticancer, and antidiabetic food additives.