The Fibrillation Kinetics of Human and Bovine Insulin Fragments and Tailored Peptides
Department
Chemical and Biochemical Engineering
Major
Chemical Engineering (Biology emphasis)
Research Advisor
Forciniti, Daniel
Advisor's Department
Chemical and Biochemical Engineering
Abstract
Amyloid deposits are insoluble proteinaceous fibrils that are responsible for diseases such as Alzheimer’s disease, type 2 diabetes and Parkinson’s disease. These proteins form clumps, due to misfolding, known as amyloid plaques that interfere with neuronal function. This study was focused on the monitoring of the kinetics of the insoluble proteins, starting from oligomers to mature fibrils. An experimental design was made to determine the main factors that contribute to fibrillation. A Thioflavin T fluorescence assay was performed to determine the presence of amyloid deposits. Afterwards, FT-IR (Fourier Transform Infrared Spectroscopy) was used to determine concentration of amyloid deposits.
Biography
Amy Snyder is a Chemical Engineering student researching under Dr. Forciniti.
Research Category
Engineering
Presentation Type
Poster Presentation
Document Type
Poster
Location
Upper Atrium/Hall
Presentation Date
15 Apr 2015, 1:00 pm - 3:00 pm
The Fibrillation Kinetics of Human and Bovine Insulin Fragments and Tailored Peptides
Upper Atrium/Hall
Amyloid deposits are insoluble proteinaceous fibrils that are responsible for diseases such as Alzheimer’s disease, type 2 diabetes and Parkinson’s disease. These proteins form clumps, due to misfolding, known as amyloid plaques that interfere with neuronal function. This study was focused on the monitoring of the kinetics of the insoluble proteins, starting from oligomers to mature fibrils. An experimental design was made to determine the main factors that contribute to fibrillation. A Thioflavin T fluorescence assay was performed to determine the presence of amyloid deposits. Afterwards, FT-IR (Fourier Transform Infrared Spectroscopy) was used to determine concentration of amyloid deposits.
