Fibrillation of Bovine and Human Insulin Fragments
Department
Chemical and Biochemical Engineering
Major
Chemical Engineering
Research Advisor
Forciniti, Daniel
Advisor's Department
Chemical and Biochemical Engineering
Abstract
Many diseases such as Alzheimer’s and Parkinson’s are linked to amyloid deposits, which are insoluble protein aggregates with a characteristic intermolecular beta-sheet structure. The buildup of these deposits is caused by the aggregation of the amyloid peptide that is found in the human body. It is known that aggregate formation damages tissue, but the kinetics of their formation is not well understood. One protein that also forms amyloid fibrils is insulin. It is known that bovine and human insulin have different fibrillation kinetics in spite of the fact of being almost identical molecules (they differ in four amino acids). In this work the fibrillation of bovine and human insulin fragments, which include the region lacking homology, was studied. Fourier Transform Infrared Spectroscopy, Transmission Electron Microscopy, and Thioflavin-T Fluorescent Spectroscopy (ThT) were used to explore the differences in kinetics of these two fragments.
Biography
Jose Morales is a senior chemical engineering student from Kansas City, MO with family roots tracing back to Mexico. Jose is interested in pursuing a career in the manufacturing industry upon his graduation this May. Jose partakes in several activities on campus besides schoolwork. He is the president of the society of Hispanic professional engineers, a member of Alpha Chi Sigma and also partakes in research. He was really interested in doing this kind of research because he felt it had real world application and it is an occurrence in his family. Jose believes that it is important to surround yourself with a variety of activities and things that interest you.
Research Category
Engineering
Presentation Type
Poster Presentation
Document Type
Poster
Location
Upper Atrium/Hall
Presentation Date
16 Apr 2014, 1:00 pm - 3:00 pm
Fibrillation of Bovine and Human Insulin Fragments
Upper Atrium/Hall
Many diseases such as Alzheimer’s and Parkinson’s are linked to amyloid deposits, which are insoluble protein aggregates with a characteristic intermolecular beta-sheet structure. The buildup of these deposits is caused by the aggregation of the amyloid peptide that is found in the human body. It is known that aggregate formation damages tissue, but the kinetics of their formation is not well understood. One protein that also forms amyloid fibrils is insulin. It is known that bovine and human insulin have different fibrillation kinetics in spite of the fact of being almost identical molecules (they differ in four amino acids). In this work the fibrillation of bovine and human insulin fragments, which include the region lacking homology, was studied. Fourier Transform Infrared Spectroscopy, Transmission Electron Microscopy, and Thioflavin-T Fluorescent Spectroscopy (ThT) were used to explore the differences in kinetics of these two fragments.
Comments
Joint project with: Jessica Randall, Alyssa Steinert