Insights into Binding Affinity of Flavonoid Compounds from Thai Herbs against 2009 H1N1 Hemagglutinin
DOI:
https://doi.org/10.48048/tis.2022.2689Keywords:
Hemagglutinin, Epicatechin gallate, Puerarin, Docking, MD simulationAbstract
Outbreak of influenza virus is one of serious concerns for public health. Hemagglutinin (HA), a spike-shaped glycoprotein on the viral surface, plays an important role during the early stage of influenza infection. In the present work, a set of flavonoids were screened against 2009 H1N1 HA by computational chemistry techniques. Among 35 flavonoids, the docking results showed that the epicatechin gallate (ECG) and puerarin exhibited a good binding affinity towards 2009 H1N1 HA. These 2 compounds were then studied by all-atom molecular dynamics (MD) simulations. The predicted binding free energy of the H1-puerarin complex (–25.86 ± 2.92 kcal/mol) was slightly greater than that of H1-ECG (–22.81 ± 2.19 kcal/mol), suggesting that the puerarin and ECG could provide similar binding affinity towards 2009 H1 HA target. However, the stronger electrostatic energy contribution of ~10 kcal/mol was found in the puerarin binding to 2009 H1N1 HA. This molecular information of ligand-protein interaction could be helpful in further drug design and development for influenza treatment.
HIGHLIGHTS
- The 35 flavonoid bioactive compounds were screened against 2009 H1N1 HA by molecular docking
- The epicatechin gallate (ECG) and puerarin exhibited a good binding affinity and were then studied by all-atom molecular dynamics (MD) simulations
- The predicted binding free energy revealed that the puerarin and ECG could provide similar binding affinity towards 2009 H1 HA target
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