A graphene oxide-based fluorescent platform for selective detection of amyloid-beta oligomers

作者:Liu Lin*; Xia Ning; Zhang Jiebin; Mao Wenhui; Wu Yangyang; Ge Xingxing
来源:Analytical Methods, 2015, 7(20): 8727-8732.
DOI:10.1039/c5ay02018b

摘要

Amyloid-beta oligomers (A beta Os) have been regarded as reliable molecular biomarkers for Alzheimer's disease (AD) diagnosis and crucial targets for therapeutic intervention. In this work, we report a graphene oxide (GO)-based fluorescence method for the selective detection of A beta Os based on the strong and specific interaction between A beta Os and the PrP(95-110) peptide, a segment of the cellular prion protein. Specifically, fluorescein isothiocyanate (FITC)-labeled PrP(95-110), denoted as FITC-PrP(95-110), was adsorbed onto the surface of GO via electrostatic and pi-pi interactions, which resulted in effective fluorescence quenching. However, in the presence of A beta Os, the competitive binding of A beta Os with GO for the peptide probe blocked the interaction between GO and FITC-PrP(95-110), which resulted in the recovery of the fluorescence signal. As a result, a detection limit of 1 nM for A beta Os (equivalent monomers) was achieved. The amenability of this method to A beta O analysis in a biological matrix was demonstrated by assaying A beta Os in artificial cerebrospinal fluid. In contrast to other reported methods for A beta O detection, our method is simple, rapid, cost-effective, highly selective, and obviates the need for a less stable antibody. We believe that our approach offers a new method for clinical diagnosis of AD and routine laboratory investigation for understanding the dynamics and mechanism of the A beta aggregation/fibrillation processes.