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Updated: Mar 22, 2026
A Tailored HPLC Purification Protocol That Yields High-purity Amyloid Beta 42 and Amyloid Beta 40 Peptides, Capable of Oligomer Formation
Published on: March 27, 2017
A new strategy to reduce amyloid deposition using peptide-imprinted membranes
Caterina Cristallini1, Elena Bellotti2, Francesca Spezia2
1CNR Institute for Polymers, Composites and Biomaterials, uos Pisa, Pisa - Italy.
Background:
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.
