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Complement-Modulating Mechanisms of Ginkgo biloba Extract in Dry AMD: Insights From Molecular Docking and Dynamics
Ting Huang1, Dan Jiang1, Dahu Wang1
1Department of Ophthalmology, Longhua Hospital Shanghai University of Traditional Chinese Medicine, Shanghai, China.
Translational Vision Science & Technology
|June 8, 2026
Summary
Ginkgo biloba extract (EGb 761) components like quercetin and ginkgolide B stabilize interactions with complement proteins C3 and C5, suggesting a therapeutic role in dry age-related macular degeneration (dry AMD). This offers a natural approach to mitigate inflammation and oxidative injury.
Area of Science:
- Ophthalmology and Pharmacology
- Computational Biology and Biochemistry
Background:
- Dry age-related macular degeneration (dry AMD) presents challenges for systemic drug delivery due to the blood-retinal barrier.
- Identifying effective bioactive compounds for ocular delivery, particularly natural compounds, is crucial for developing novel therapeutics.
- Ginkgo biloba extract (EGb 761) is a clinically validated extract with demonstrated safety and efficacy in ophthalmology.
Purpose of the Study:
- To elucidate the complement-modulating mechanisms of Ginkgo biloba extract (EGb 761) in dry age-related macular degeneration (dry AMD).
- To investigate the binding interactions of EGb 761 components with key complement proteins C3 and C5 using computational methods.
Main Methods:
- Bioinformatics analysis to identify dry AMD-related targets.
- Molecular docking and 100-ns molecular dynamics (MD) simulations to assess binding stability and free energy.
- MM-Poisson-Boltzmann surface area analysis to determine binding contributions and identify critical residues.
Main Results:
- Quercetin and ginkgolide B exhibited the strongest and most stable binding with complement proteins C3 and C5.
- Persistent hydrogen bond networks and significant van der Waals/electrostatic interactions were observed.
- Key residues in C3 (ASP1435, GLU1433, LYS1001, LYS1436) and C5 (ASP1457, GLU837, GLU932) were identified as critical binding hotspots.
Conclusions:
- Major active components of EGb 761 act as natural complement modulators by stabilizing interactions with C3 and C5.
- This mechanism suggests potential for mitigating inflammation and oxidative injury in dry AMD.
- Provides a mechanistic basis for EGb 761's therapeutic potential and informs development of natural complement-targeting agents.
