Predicting the Combined Effect of Quercetin and Kaempferol on the Folding Stability of the D90A SOD1 Mutant by Molecular Docking
School Name
Spring Valley High School
Grade Level
11th Grade
Presentation Topic
Biochemistry
Presentation Type
Non-Mentored
Abstract
Amyotrophic Lateral Sclerosis (ALS) is a fatal and progressive neurodegenerative disease. Some causes are linked to the misfolding of proteins such as superoxide dismutase 1 (SOD1) due to mutations (like D90A) in the gene. Protein misfolding can disrupt functions of cells and contribute to motor neuron degeneration. Flavonoids are plant-based compounds that have many beneficial properties such as neuroprotection and antioxidation, and their effects have been tested on SOD1 as well as other proteins. Two flavonoids, quercetin and kaempferol exhibit these properties, but their combined effect on the D90A mutant of the SOD1 gene has not been examined. This research uses AutoDock Vina to conduct molecular docking and acquire estimated binding affinity (docking) scores of quercetin and kaempferol separately, and then used a combined additive model to to approximate their dual effect due to software limitations. The results showed a mean binding affinity score of -6.83 kcal/mol for quercetin, -6.77 kcal/mol for kaempferol, and -13.6 kcal/mol for the combined additive model. Results suggested a stronger estimated binding for the combined additive model (more negative = stronger). A one-way ANOVA test was run and then confirmed statistically significant differences between the groups (F(2, 87) = 196.46, p < .001). A post hoc Tukey HSD test was then run and determined that the combined additive model was the group that was statistically significantly different from the other groups. The findings indicate a predicted potential for quercetin and kaempferol in combination to stabilize the D90A SOD1 mutant misfolding, which provides a computational foundation for further experimental studies.
Recommended Citation
Kuhn, Duncan, "Predicting the Combined Effect of Quercetin and Kaempferol on the Folding Stability of the D90A SOD1 Mutant by Molecular Docking" (2026). South Carolina Junior Academy of Science. 45.
https://scholarexchange.furman.edu/scjas/2026/all/45
Location
Furman Hall 107
Start Date
3-28-2026 11:15 AM
Presentation Format
Oral and Written
Group Project
No
Predicting the Combined Effect of Quercetin and Kaempferol on the Folding Stability of the D90A SOD1 Mutant by Molecular Docking
Furman Hall 107
Amyotrophic Lateral Sclerosis (ALS) is a fatal and progressive neurodegenerative disease. Some causes are linked to the misfolding of proteins such as superoxide dismutase 1 (SOD1) due to mutations (like D90A) in the gene. Protein misfolding can disrupt functions of cells and contribute to motor neuron degeneration. Flavonoids are plant-based compounds that have many beneficial properties such as neuroprotection and antioxidation, and their effects have been tested on SOD1 as well as other proteins. Two flavonoids, quercetin and kaempferol exhibit these properties, but their combined effect on the D90A mutant of the SOD1 gene has not been examined. This research uses AutoDock Vina to conduct molecular docking and acquire estimated binding affinity (docking) scores of quercetin and kaempferol separately, and then used a combined additive model to to approximate their dual effect due to software limitations. The results showed a mean binding affinity score of -6.83 kcal/mol for quercetin, -6.77 kcal/mol for kaempferol, and -13.6 kcal/mol for the combined additive model. Results suggested a stronger estimated binding for the combined additive model (more negative = stronger). A one-way ANOVA test was run and then confirmed statistically significant differences between the groups (F(2, 87) = 196.46, p < .001). A post hoc Tukey HSD test was then run and determined that the combined additive model was the group that was statistically significantly different from the other groups. The findings indicate a predicted potential for quercetin and kaempferol in combination to stabilize the D90A SOD1 mutant misfolding, which provides a computational foundation for further experimental studies.