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Investigation of flexibility of neuraminidase 150-loop using tamiflu derivatives in influenza A viruses H1N1 and H5N1.

Bioorg. Med. Chem.. 2019-07; 
ZimaVáclav,AlbiñanaCarlos Berenguer,RojíkováKateřina,PokornáJana,PachlPetr,ŘezáčováPavlína,HudlickyJason,NavrátilVáclav,MajerPavel,KonvalinkaJan,KožíšekMilan,MacharaA
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Molecular Biology Reagents DNAs encoding the ectodomain of neuraminidase (residues 82–469) from the A/California/07/2009 (H1N1) and A/chicken/NakornPatom/Thailand/CU-K2/2004 (H5N1) influenza virus were prepared by GenScript USA Inc. (Genbank Source Sequence CY121682 and AY590567, respectively). Get A Quote

摘要

This study focuses on design, synthesis and in vitro evaluation of inhibitory potency of two series of sialylmimetic that target an exosite ("150-cavity") adjacent to the active site of influenza neuraminidases from A/California/07/2009 (H1N1) pandemic strain and A/chicken/Nakorn-Patom/Thailand/CU-K2-2004 (H5N1). The structure-activity analysis as well as 3-D structure of the complex of parental compound with the pandemic neuraminidase p09N1 revealed high flexibility of the 150-cavity towards various modification of the neuraminidase inhibitors. Furthermore, our comparison of two methods for inhibition constant determination performed at slightly different pH values suggest that the experimental conditions ... More

关键词

Click chemistry,Crystal structure,Influenza neuraminidase,Oseltam