2016 AIChE Annual Meeting

(391c) Influence of Gold Nanoparticle Surface Chemistry and Diameter upon Alzheimer’s Disease Amyloid-β Protein Aggregation

Authors

Melissa A. Moss - Presenter, University of South Carolina
Kayla Pate, University of South Carolina
Deborah Soto-Ortega, University of South Carolina
Sam Lohse, University of Illinois at Urbana-Champaign
Nicholas van der Munnik, University of South Carolina
Mihyun Lim, University of South Carolina
Kelly A. Moore, University of South Carolina
Kaliah Jackson, SC State University
Mark J. Uline, University of South Carolina
Rahina Mahtab, SC State University
Catherine Murphy, University of Illinois at Urbana-Champaign
Venetia Lyles, South Carolina State University
Lemeisha Jones, South Carolina State University
Deposits of aggregated amyloid-β protein (Aβ) are a pathological hallmark of Alzheimerâ??s disease (AD). Thus, one therapeutic strategy is to eliminate these deposits by halting Aβ aggregation. While a variety of possible aggregation inhibitors have been explored, only nanoparticles (NPs) exhibit promise at low substoichiometric ratios. With tunable size, shape, and surface properties, NPs present an ideal platform for rationally designed Aβ aggregation inhibitors. In this study, we characterized the inhibitory capabilities of gold nanospheres exhibiting different surface coatings and diameters. Both diameter and surface chemistry were found to modulate the extent of aggregation, while NP electric charge influenced aggregate morphology. Notably, 8 nm and 18 nm poly(acrylic acid) NPs abrogated Aβ aggregation at a substoichiometric ratio of 1:2,000,000. Theoretical calculations suggest that this stoichiometry could arise from altered solution conditions near the NP surface. Insights provided by this study will inform future rational design of effective NP-based therapeutics for AD.