Hesperidin as a Multi-Target Flavonoid
Hesperidin is a flavonoid evaluated by AMH Biotech LLC using integrated computational and experimental methodologies.
Research findings suggest that Hesperidin interacts with multiple biologically relevant protein systems.
TMPRSS2 Interaction
Docking studies demonstrated:
- Active-site engagement
- Catalytic triad interaction
- Stable hydrogen bonding
- Favorable binding geometry
TMPRSS2 inhibition assays further supported functional interaction.
SARS-CoV-2 Mpro Interaction
Hesperidin also demonstrated stable interaction within the SARS-CoV-2 main protease (Mpro) pocket.
Interaction mapping identified:
- Hydrogen bonding
- Hydrophobic stabilization
- Multi-point pocket occupancy
Spike Protein Interaction
Moderate interaction patterns were observed within structurally relevant regions of the Spike receptor-binding domain.
Influenza Hemagglutinin (HA)
Additional docking studies demonstrated moderate Hesperidin interaction with influenza hemagglutinin.
The interaction profile suggested potential influence on protein conformational behavior associated with viral entry.
Surface Plasmon Resonance (SPR)
SPR experiments demonstrated measurable ligand-protein interaction behavior and supported the computational findings.
Integrated Research Workflow
The Hesperidin antiviral evaluation framework developed by AMH Biotech includes:
- AutoDock Vina molecular docking
- LigPlot+ interaction analysis
- Surface Plasmon Resonance
- TMPRSS2 inhibition assays
- Calu-3 cell validation systems
Scientific Positioning
The Hesperidin research program emphasizes:
- Mechanism-based analysis
- Multi-target interaction evaluation
- Structured experimental validation
- High-purity flavonoid investigation
AMH - BIOTECH
