As a powerful analytical technique harnessing optical, microscopy, and electronics components, single-molecule fluorescence spectroscopy affords valuable and unique learning opportunities in the undergraduate chemistry curriculum. Following from research in our laboratory, undergraduates in Instrumental Analysis employ single-particle fluorescence to monitor the oligomerization of dye-labeled amyloid-� (A�) peptides. A� dimers, trimers, and tetramers are linked to synapse loss and memory deficits in Alzheimer's disease. Exploiting quantized photobleaching, students quantify the number of associated peptides (n = 1-5) in individual, surface-tethered oligomers. Student pairs spend one laboratory period acquiring fluorescence intensity trajectories for dozens of A� peptide species; the following period is devoted to data-processing and analysis, after which each pair generates an oligomer distribution for the sample environment they investigated. Statistical analyses of distributions from all pairs permit comparison of various physiologically relevant sample environments and assessment of reproducibility across multiple samples.

Single-nanoparticle spectroscopy in the Instrumental Analysis Laboratory: Quantifying oligomers of Alzheimer's amyloid-β peptide

244th National Meeting (2012)

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