Title

Fibrillation of Bovine and Human Insulin Fragments

Presenter Information

Jessica Randall

Department

Chemical and Biochemical Engineering

Major

Chemical 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

Jessica Randall is a student from Lee’s Summit, MO pursuing a Bachelor’s Degree in Chemical Engineering. She currently holds an undergraduate research assistant position working under the tutelage of Dr. Forciniti. Her areas of research specialty are in peptide synthesis and characterization using Fourier Transform Infrared Spectroscopy. She plans to graduate in May of 2014 and pursue a career in process chemical engineering.

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, Alyssa Steinert

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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.