Peptide-Functionalized Magnetically-Active Nanoparticles for Targeted Manipulation of Amyloid Fibrils
Mentor/s
Dr. Benjamin Alper, Chemistry Department
Participation Type
Poster
Abstract
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.
College and Major available
Chemistry
Location
University Commons
Start Day/Time
4-20-2018 1:00 PM
End Day/Time
4-20-2018 3:00 PM
Creative Commons License
This work is licensed under a Creative Commons Attribution-Noncommercial-Share Alike 4.0 License.
Prize Categories
Most Scholarly Impact or Potential, Most Creative, Most Meaningful
Peptide-Functionalized Magnetically-Active Nanoparticles for Targeted Manipulation of Amyloid Fibrils
University Commons
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.
