Real-time Amyloid Aggregation Monitoring with a Photonic Crystal-based Approach
Author(s)
Musi, Valeria
Descrovi, Emiliano
Paeder, Vincent
Hvozdara, Lubos
van der Wal, Peter
Lashuel, Hilal A.
Pastore, Annalisa
Herzig, Hans Peter
Date issued
2013
In
ChemPhysChem
Vol
15
No
14
From page
3476
To page
3482
Subjects
Optical sensors (biosensors refractive index real-time amyloid aggregation monitoring with photonic crystal-based approach) Surface wave (bloch real-time amyloid aggregation monitoring with photonic crystal-based approach) Organelle (fibril real-time amyloid aggregation monitoring with photonic crystal-based approach) Adsorption (interfacial real-time amyloid aggregation monitoring with photonic crystal-based approach) Polymerization (oligomerization real-time amyloid aggregation monitoring with photonic crystal-based approach) Biosensors (optical refractive index real-time amyloid aggregation monitoring with photonic crystal-based approach) Aggregation Photonic crystals Refractive index Refractometers Self-assembled monolayers Simulation and Modeling Surface treatment (real-time amyloid aggregation monitoring with photonic crystal-based approach) Polyoxyalkylenes Role: ARU (Analytical role unclassified) BUU (Biological use unclassified) PEP (Physical engineering or chemical process) TEM (Technical or engineered material use) ANST (Analytical study) BIOL (Biological study) PROC (Process) amyloid aggregation biosensor refractometry photonic crystal
Abstract
We propose the application of a new label-free optical technique based on photonic nanostructures to real-time monitor the amyloid-beta 1-42 (A?(1-42)) fibrillization, including the early stages of the aggregation process, which are related to the onset of the Alzheimer's Disease (AD). The aggregation of A? peptides into amyloid fibrils has commonly been assocd. with neuronal death, which culminates in the clin. features of the incurable degenerative AD. Recent studies revealed that cell toxicity is detd. by the formation of sol. oligomeric forms of A? peptides in the early stages of aggregation. At this phase, classical amyloid detection techniques lack in sensitivity. Upon a chem. passivation of the sensing surface by means of polyethylene glycol, the proposed approach allows an accurate, real-time monitoring of the refractive index variation of the soln., wherein A?(1-42) peptides are aggregating. This measurement is directly related to the aggregation state of the peptide throughout oligomerization and subsequent fibrillization. Our findings open new perspectives in the understanding of the dynamics of amyloid formation, and validate this approach as a new and powerful method to screen aggregation at early stages. [on SciFinder(R)]
Publication type
journal article
