Title

Fibrillation of Bovine and Human Insulin Fragments

Presenter Information

Alyssa Steinert

Department

Chemical and Biochemical Engineering

Major

Biochemical Engineering

Research Advisor

Forciniti, Daniel

Advisor's Department

Chemical and Biochemical Engineering

Funding Source

Opportunities for Undergraduate Experience Program (OURE)

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

Alyssa Steinert is a senior from Ozark, MO pursuing a degree in Chemical Engineering with an emphasis in Biochemical Engineering. Along with focusing on her studies, Alyssa also participates in many organizations on campus. She is currently a Certified Peer Educator for Joe's PEERS, a member of both Alpha Chi Sigma and American Institute of Chemical Engineers, and she partakes in research under the guidance of Dr. Forciniti. She plans to pursue a career in Chemical Engineering upon her graduation in May.

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

Comments

Joint project with Jose Morales, Jessica Randall

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Apr 16th, 1:00 PM Apr 16th, 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.