Exploration of Binding Mechanism of a Potential Neuraminidase Inhibitor from Herbaceous Plants by Molecular Simulation.

can cause diseases such as pneumonia. Broad-spectrum antibiotic therapy for is increasingly limited due to the emergence of drug-resistant strains. The development of novel drugs is still currently of focus. Abundant polyphenols have been demonstrated to have antivirus and antibacterial ability. Chlorogenic acid is one of the representatives that has been proven to have the potential to inhibit both the influenza virus and . However, for such a potential neuraminidase inhibitor, the interaction mechanism studies between chlorogenic acid and neuraminidase are rare. In the current study, the binding mechanism of chlorogenic acid and neuraminidase were investigated by molecular simulation. The results indicated that chlorogenic acid might establish the interaction with neuraminidase via hydrogen bonds, salt bridge, and cation-π. The vital residues involved Arg347, Ile348, Lys440, Asp372, Asp417, and Glu768. The side chain of Arg347 might form a cap-like structure to lock the chlorogenic acid to the active site. The results from binding energy calculation indicated that chlorogenic acid had strong binding potential with neuraminidase. The results predicted a detailed binding mechanism of a potential neuraminidase inhibitor, which will be provide a theoretical basis for the mechanism of new inhibitors.