The amyloid hypothesis asserts that accumulation of amyloid beta (Aβ) peptides is a primary cause of Alzheimer’s disease. This project seeks to identify novel strategies for disruption or elimination of amyloid fibrils through development of peptide-functionalized magnetically-active nanoparticles. Water-soluble polyethylene oxide-stabilized iron oxide nanoparticles (PEO-IONPs) were conjugated through azide “click” chemistry to short, hydrophobic KLVFFAL peptides approximating the minimal sufficient Aβ peptide fibril nucleation motif (i.e., yielding KLVFFAL-PEO-IONPs).  Experimental efforts sought to incorporate this particle within elongating amyloid fibrils, with peptide aggregation assessed by thioflavin T fluorescence assay. Amyloid peptide aggregation was observed in the presence and in the absence of KLVFFAL-PEO-IONPs. Preliminary data suggest that amyloid fibril partitioning was achieved in the presence of KLVFFAL-PEO-IONPs subject to application of a magnetic field.<br/>

Peptide-functionalized magnetically-active nanoparticles for targeted manipulation of amyloid fibrils

255th National Meeting (2018)

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