Determining Secondary Structure Relation to Singlet Oxygen Reaction Rates with Eye Lens Protective Proteins α-Crystallin, β-Crystallin, and γ-Crystallin
Location
CSU Ballroom
Start Date
10-4-2018 10:00 AM
End Date
10-4-2018 11:30 AM
Student's Major
Biological Sciences
Student's College
Science, Engineering and Technology
Mentor's Name
John Thoemke
Mentor's Department
Biological Sciences
Mentor's College
Science, Engineering and Technology
Description
Ninety percent of the lens proteins of the human eye lens consist of Crystallin proteins, which are important in the prevention of protein aggregation. Fully mature lens fiber cells do not produce or degrade proteins, therefore existing proteins must remain stable in solution for the lifetime of the individual. With any denaturation of Crystallin proteins the protective function fails causing protein aggregation, subsequent blurring of the lens, and the patient develops cataracts. Singlet oxygen is a common denaturation agent of proteins. This highly reactive form of oxygen reacts with protein molecules, causing structural changes. These structural changes can be detected using molecular probes, HPLC, and fluorescence spectroscopy. HPLC measurements coupled with molecular probes have shown that α-Crystallin is more reactive with singlet oxygen than γ-Crystallin. This coincides with our hypothesis that α-Crystallin should react faster than γ-Crystallin due to the presence of more tryptophan amino acids. The faster reaction with singlet oxygen and α-Crystallin should cause more denaturation, as observed using fluorescence spectroscopy. The combined results from probe molecules, HPLC, and Fluorescence spectroscopy, along with the primary amino acid sequences have allowed the identification of specific structures within the Crystallin proteins that increase or decrease the rate of singlet oxygen damage. This information can be used to better understand why certain proteins develop cataracts more readily than others.
Determining Secondary Structure Relation to Singlet Oxygen Reaction Rates with Eye Lens Protective Proteins α-Crystallin, β-Crystallin, and γ-Crystallin
CSU Ballroom
Ninety percent of the lens proteins of the human eye lens consist of Crystallin proteins, which are important in the prevention of protein aggregation. Fully mature lens fiber cells do not produce or degrade proteins, therefore existing proteins must remain stable in solution for the lifetime of the individual. With any denaturation of Crystallin proteins the protective function fails causing protein aggregation, subsequent blurring of the lens, and the patient develops cataracts. Singlet oxygen is a common denaturation agent of proteins. This highly reactive form of oxygen reacts with protein molecules, causing structural changes. These structural changes can be detected using molecular probes, HPLC, and fluorescence spectroscopy. HPLC measurements coupled with molecular probes have shown that α-Crystallin is more reactive with singlet oxygen than γ-Crystallin. This coincides with our hypothesis that α-Crystallin should react faster than γ-Crystallin due to the presence of more tryptophan amino acids. The faster reaction with singlet oxygen and α-Crystallin should cause more denaturation, as observed using fluorescence spectroscopy. The combined results from probe molecules, HPLC, and Fluorescence spectroscopy, along with the primary amino acid sequences have allowed the identification of specific structures within the Crystallin proteins that increase or decrease the rate of singlet oxygen damage. This information can be used to better understand why certain proteins develop cataracts more readily than others.
Recommended Citation
Allen, Cody. "Determining Secondary Structure Relation to Singlet Oxygen Reaction Rates with Eye Lens Protective Proteins α-Crystallin, β-Crystallin, and γ-Crystallin." Undergraduate Research Symposium, Mankato, MN, April 10, 2018.
https://cornerstone.lib.mnsu.edu/urs/2018/poster-session-A/23
