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Detecting Amyloid-β Aggregation with Fiber-Based Fluorescence Correlation Spectroscopy

Kanchan Garai ^*, Ruchi Sureka  and S. Maiti ^*

^* Tata Institute of Fundamental Research, Colaba, Mumbai, India; and Manipal Academy of Higher Education, Manipal, Karnataka, India

Correspondence: Address reprint requests and inquiries to Sudipta Maiti, Tel.: 091-222-278-2716; Fax: 091-222-280-4610; E-mail: maiti{at}tifr.res.in.

Soluble aggregates critically influence the chemical and biological aspects of amyloid protein aggregation, but their population is difficult to measure, especially in vivo. We take an optical fiber-based fluorescence correlation spectroscopy (FCS) approach to characterize a solution of aggregating amyloid-β molecules. We find that this technique can easily resolve aggregate particles of size 100 nm or greater in vitro, and the size distribution of these particles agrees well with that obtained by conventional FCS techniques. We propose fiber FCS as a tool for studying aggregation in vivo.