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Size and Flexibility Define the Inhibition of the H3N2 Influenza Endonuclease Enzyme by Calix[n]arenes

2019; Multidisciplinary Digital Publishing Institute; Volume: 8; Issue: 2 Linguagem: Inglês

10.3390/antibiotics8020073

2079-6382

Yannick Tauran, José P. Cerón‐Carrasco, Moez Rhimi, Florent Perret, Beomjoon Kim, Dominique Collard, Anthony W. Coleman, Horacio Pérez‐Sánchez,

RNA and protein synthesis mechanisms

Inhibition of H3N2 influenza PA endonuclease activity by a panel of anionic calix[n]arenes and β-cyclodextrin sulfate has been studied. The joint experimental and theoretical results reveal that the larger, more flexible and highly water-soluble sulfonato-calix[n]arenes have high inhibitory activity, with para-sulfonato-calix[8]arene, SC8, having an IC50 value of 6.4 μM. Molecular docking calculations show the SC8 can interact at both the polyanion binding site and also the catalytic site of H3N2 influenza PA endonuclease.