The accumulation of amyloid beta protein in the brain causes the cognitive impairment observed in neurodegenerative pathologies such as Alzheimer's disease. The present study aimed to test the hypothesis that a rapid removal of amyloid beta protein peptides from the blood by an extracorporeal purification system could represent an alternative solution for the treatment of patients suffering from this neurodegenerative disease.Methods:
In this regard, we investigated the specific recognition properties of a molecularly imprinted membrane based on poly(ethylene-co-vinyl alcohol) toward the amyloid beta protein fragment 25-35 (AbP), the more neurotoxic domain of amyloid beta protein. A chemical modification of the copolymer backbone using succinic anhydride was also performed to favor the formation of carboxylic groups and thus improve imprinting performance.Results:
The physico-chemical, morphological, mechanical and functional characterisations gave interesting results confirming the ability of imprinted membranes to in vitro rebind AbP.Conclusions:
This work represents a proof of concept regarding the development of a biocompatible polymer membrane capable of selectively removing amyloid beta peptide from the blood and consequently from the cerebrospinal fluid.