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The aggregation of A\u03b2 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 A\u03b2 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\u2010time monitoring of the refractive index variation of the solution, wherein A\u03b2(1\u201042) 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.<\/jats:p>","DOI":"10.1002\/cphc.201300633","type":"journal-article","created":{"date-parts":[[2013,10,4]],"date-time":"2013-10-04T05:41:42Z","timestamp":1380865302000},"page":"3476-3482","update-policy":"https:\/\/doi.org\/10.1002\/crossmark_policy","source":"Crossref","is-referenced-by-count":26,"title":["Real\u2010time Amyloid Aggregation Monitoring with a Photonic Crystal\u2010based 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