Belfort Group

Biomolecular Separations Research Group
Howard P. Isermann Department of Chemical and Biological Engineering
and Center for Biotechnology and Interdisciplinary Studies
Rensselaer Polytechnic Institute
Troy, NY 12180, USA

The Kinetics of Nucleation and Growth of Amyloidogenic Proteins

One of several proposed causes of Alzheimer's Disease (AD) is the disruption and resulting ion leakage of cell membranes. Since amyloid beta peptide (Aβ1-42), a peptide strongly implicated in the pathogenesis of AD, is known to interact with hydrophobic species including mammalian cell membranes and glutamate receptors, we are studying this process in great detail. We use a model lipid bilayer comprising components of mammalian cell membranes and a patch clamp method to determine the disruption of calcium transport through the glutamate receptor. We also compare Aβ1-42 disruption with those of antimicrobial peptides and bacterial lipid bilayers.

Previous research focused on amyloid aggregation and how the presence of multiple crowding agents influenced the rate of aggregation. Altering solution conditions, such as viscosity, with crowding agents, or specific interactions between crowders and amyloidogenic proteins play the largest role in determining the change in rate of amyloid aggregation. We collaborate with Payel Das, IBM.