Real-time protein aggregation monitoring with a Bloch surface wave-based approach

Hans Peter Herzig, Sara Santi
Spie-Int Soc Optical Engineering, 2014
Conference paper

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Hans Peter Herzig, Sara Santi
Spie-Int Soc Optical Engineering, 2014
Conference paper

Abstract

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https://infoscience.epfl.ch/record/202058?ln=en

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Real-time Protein Aggregation Monitoring with a Bloch Surface Wavebased Approach

Elsie Barakat, Hans Peter Herzig, Sara Santi

The misfolding and aggregation of amyloid proteins has been associated with incurable diseases such as Alzheimer's or Parkinson's disease. In the specific case of Alzheimer's disease, recent studies have shown that cell toxicity is caused by soluble oligomeric forms of aggregates appearing in the early stages of aggregation, rather than by insoluble fibrils. Research on new strategies of diagnosis is imperative to detect the disease prior to the onset of clinical symptoms. Here, we propose the use of an optical method for protein aggregation dynamic studies using a Bloch surface wave based approach. A one dimension photonic crystal made of a periodic stack of silicon oxide and silicon nitride layers is used to excite a Bloch surface wave, which is sensitive to variation of the refractive index of an aqueous solution. The aim is to detect the early dynamic events of protein aggregation and fibrillogenesis of the amyloid-beta peptide Aβ42, which plays a central role in the onset of the Alzheimer’s disease. The detection principle relies on the refractive index changes caused by the depletion of the Aβ42 monomer concentration during oligomerization and fibrillization. We demonstrate the efficacy of the Bloch surface wave approach by monitoring in real-time the first crucial steps of Aβ42 oligomerization.

Spie-Int Soc Optical Engineering2014

Real-time Amyloid Aggregation Monitoring with a Photonic Crystal-based Approach

Joab Di Francesco, Hans Peter Herzig, Lubos Hvozdara, Hilal Lashuel, Valeria Musi, Vincent Paeder, Sara Santi, Peter Van der Wal

We propose the application of a new label-free optical technique based on photonic nanostructures to real-time monitor the amyloid-beta 1-42 (Ab(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 Ab peptides into amyloid fibrils has commonly been associated with neuronal death, which culminates in the clinical features of the incurable degenerative AD. Recent studies revealed that cell toxicity is determined by the formation of soluble oligomeric forms of Ab peptides in the early stages of aggregation. At this phase, classical amyloid detection techniques lack in sensitivity. Upon a chemical 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 solution, wherein A beta(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

Wiley-Blackwell2013