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Binding of blockers to the Influenza A ion-channel is studied using automated docking calculations. Our study suggests that studied cage compounds inhibit the M2 ion channel by binding to the His37 residue. The adamantane cage fits into a pocket formed by Trp41 residue, while the hydrogen bond is formed between hydrogen atom of ammonium nitrogen and the nitrogen of histidine residue. This finding is supported by experimental data and should help to obtain better understanding of the inhibition mechanism of the Influenza A M2 ion channel.

Mechanism of Influenza A M2 Ion-Channel Inhibition: A Docking and QSAR Study