Title

Surface Properties that Catalyze Amyloid Fibril Formation

Presenter Information

Morgan Boresi

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

Comments

Joint project with Paulina Barranco and Cuong Pham

This document is currently not available here.

Share

COinS
 
Apr 7th, 1:00 PM Apr 7th, 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.