tetano
Editor, Senior Moderator
Yao Xue Xue Bao. 2011 Nov;46(11):1344-8.
[Design, synthesis and activity of a new type of influenza virus N1 neuraminidase inhibitors].
[Article in Chinese]
Yang F, Jin L, Huang NY, Chen F, Luo HJ, Chen JF.
Source
Hubei Key Laboratory of Natural Products Research and Development, China Three Gorges University, Yichang 443002, China.
Abstract
In this study, the "150-cavity", next to the H5N1 influenza virus neuraminidase activity site, has been used as the target to design and synthesize a structural analogue of chlorogenic acid, N-caffeoyl-GABA, using the flexible docking simulation. The docking study showed that the N-caffeoyl-GABA could be inserted into the "150-cavity" and combined with the Arg156 side chain by hydrogen bond. The best binding free energy of H5N1 NA-N-caffeoyl-GABA complex was -7.70 kcal mol(-1), equivalent that of the NA-oseltamivir. At the same time, using the H5N1 pseudotyping virus-based NA inhibitors screening model, we determined the inhibitory effect of oseltamivir, chlorogenic acid and N-caffeoyl-GABA on the NA. Compared with chlorogenic acid, N-caffeoyl-GABA significantly enhanced the inhibitory effect on NA, but less than oseltamivir. This study showed that the "150-cavity" could possibly be used as a new neuraminidase inhibitors target, and provided a path for the development of new neuraminidase inhibitors.
PMID:
22260026
[PubMed - in process]
http://www.ncbi.nlm.nih.gov/pubmed/22260026
[Design, synthesis and activity of a new type of influenza virus N1 neuraminidase inhibitors].
[Article in Chinese]
Yang F, Jin L, Huang NY, Chen F, Luo HJ, Chen JF.
Source
Hubei Key Laboratory of Natural Products Research and Development, China Three Gorges University, Yichang 443002, China.
Abstract
In this study, the "150-cavity", next to the H5N1 influenza virus neuraminidase activity site, has been used as the target to design and synthesize a structural analogue of chlorogenic acid, N-caffeoyl-GABA, using the flexible docking simulation. The docking study showed that the N-caffeoyl-GABA could be inserted into the "150-cavity" and combined with the Arg156 side chain by hydrogen bond. The best binding free energy of H5N1 NA-N-caffeoyl-GABA complex was -7.70 kcal mol(-1), equivalent that of the NA-oseltamivir. At the same time, using the H5N1 pseudotyping virus-based NA inhibitors screening model, we determined the inhibitory effect of oseltamivir, chlorogenic acid and N-caffeoyl-GABA on the NA. Compared with chlorogenic acid, N-caffeoyl-GABA significantly enhanced the inhibitory effect on NA, but less than oseltamivir. This study showed that the "150-cavity" could possibly be used as a new neuraminidase inhibitors target, and provided a path for the development of new neuraminidase inhibitors.
PMID:
22260026
[PubMed - in process]
http://www.ncbi.nlm.nih.gov/pubmed/22260026