tetano
Editor, Senior Moderator
Antibiotics (Basel). 2019 Jun 3;8(2). pii: E73. doi: 10.3390/antibiotics8020073.
[h=1]Size and Flexibility Define the Inhibition of the H3N2 Influenza Endonuclease Enzyme by Calix[n]arenes.[/h] Tauran Y[SUP]1,[/SUP][SUP]2[/SUP], Cer?n-Carrasco JP[SUP]3[/SUP], Rhimi M[SUP]4[/SUP], Perret F[SUP]5[/SUP], Kim B[SUP]6,[/SUP][SUP]7[/SUP], Collard D[SUP]8[/SUP], Coleman AW[SUP]9[/SUP], P?rez-S?nchez H[SUP]10[/SUP].
[h=3]Author information[/h]
[h=3]Abstract[/h] 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 IC[SUB]50[/SUB] 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.
[h=4]KEYWORDS:[/h] H3N2 virus; anti-viral activity; calix[n]arene; endonuclease; enzyme inhibitors; molecular docking
PMID: 31163674 DOI: 10.3390/antibiotics8020073
Free full text
[h=1]Size and Flexibility Define the Inhibition of the H3N2 Influenza Endonuclease Enzyme by Calix[n]arenes.[/h] Tauran Y[SUP]1,[/SUP][SUP]2[/SUP], Cer?n-Carrasco JP[SUP]3[/SUP], Rhimi M[SUP]4[/SUP], Perret F[SUP]5[/SUP], Kim B[SUP]6,[/SUP][SUP]7[/SUP], Collard D[SUP]8[/SUP], Coleman AW[SUP]9[/SUP], P?rez-S?nchez H[SUP]10[/SUP].
[h=3]Author information[/h]
[h=3]Abstract[/h] 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 IC[SUB]50[/SUB] 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.
[h=4]KEYWORDS:[/h] H3N2 virus; anti-viral activity; calix[n]arene; endonuclease; enzyme inhibitors; molecular docking
PMID: 31163674 DOI: 10.3390/antibiotics8020073
Free full text