• Thanyada Rungrotmongkol, Pathumwadee Intharathep, Maturos Malaisree, Nadtanet Nunthaboot, Nopphorn Kaiyawet, Pornthep Sompornpisut, Sanchai Payungporn, Yong Poovorawan, and Supot Hannongbua.
• Department of Chemistry, Faculty of Science, Chulalongkorn University, Phayathai Road, Patumwan, Bangkok 10330, Thailand.
• Biochem. Biophys. Res. Commun. 2009 Jul 31;385(3):390-4.

AbstractThe recent outbreak of the novel strain of influenza A (H1N1) virus has raised a global concern of the future risk of a pandemic. To understand at the molecular level how this new H1N1 virus can be inhibited by the current anti-influenza drugs and which of these drugs it is likely to already be resistant to, homology modeling and MD simulations have been applied on the H1N1 neuraminidase complexed with oseltamivir, and the M2-channel with adamantanes bound. The H1N1 virus was predicted to be susceptible to oseltamivir, with all important interactions with the binding residues being well conserved. In contrast, adamantanes are not predicted to be able to inhibit the M2 function and have completely lost their binding with the M2 residues. This is mainly due to the fact that the M2 transmembrane of the new H1N1 strain contains the S31N mutation which is known to confer resistance to adamantanes.

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