Surface Properties that Catalyze Amyloid Fibril Formation
Department
Chemical and Biochemical Engineering
Major
Chemical Engineering
Research Advisor
Forciniti, Daniel
Advisor's Department
Chemical and Biochemical Engineering
Funding Source
National Science Foundation
Abstract
Amyloid fibrils are found in many diseases such as Alzheimer’s Disease, Parkinson’s Disease, Huntington’s Disease, Type 2 Diabetes, Rheumatoid Arthritis, and many more. These fibrils are protein aggregates with a characteristic β-sheet formation, which binds Congo Red. It is possible that the formation of amyloid deposits is “catalyzed” by solid liquid interfaces. In this experiment the rate and extent of aggregation of bovine insulin was determined in the presence of several different surfaces. The experiments were design to deepen our knowledge about the formation of amyloid deposits without which limited progress may be achieve in finding cures for these devastating diseases. The chemistry of surfaces was chosen to mimic those surfaces found in cells. The rate of aggregation was followed by dynamic light scattering, which was used to monitor the aggregate size as a function of time. Congo Red assays were performed to confirm if the aggregates were amyloidic.
Biography
Morgan Boresi is a senior graduating in May with a degree in Chemical Engineering with an emphasis in Biology and minors in Biology and Psychology Neuroscience. She works in Dr. Daniel Forciniti’s laboratory as an undergraduate research assistant. Outside of research she participates in several student organizations including Kappa Delta Sorority, Panhellenic Council, and AIChE. After graduation she plans to attend graduate school at Arizona State University to earn a PhD. in Bioengineering.
Research Category
Engineering
Presentation Type
Poster Presentation
Document Type
Poster
Location
Upper Atrium/Hallway
Presentation Date
07 Apr 2010, 1:00 pm - 3:00 pm
Surface Properties that Catalyze Amyloid Fibril Formation
Upper Atrium/Hallway
Amyloid fibrils are found in many diseases such as Alzheimer’s Disease, Parkinson’s Disease, Huntington’s Disease, Type 2 Diabetes, Rheumatoid Arthritis, and many more. These fibrils are protein aggregates with a characteristic β-sheet formation, which binds Congo Red. It is possible that the formation of amyloid deposits is “catalyzed” by solid liquid interfaces. In this experiment the rate and extent of aggregation of bovine insulin was determined in the presence of several different surfaces. The experiments were design to deepen our knowledge about the formation of amyloid deposits without which limited progress may be achieve in finding cures for these devastating diseases. The chemistry of surfaces was chosen to mimic those surfaces found in cells. The rate of aggregation was followed by dynamic light scattering, which was used to monitor the aggregate size as a function of time. Congo Red assays were performed to confirm if the aggregates were amyloidic.
Comments
Joint project with Paulina Barranco and Cuong Pham