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.

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Apr 10th, 10:00 AM Apr 10th, 11:30 AM

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