tetano
Editor, Senior Moderator
Bioorg Med Chem. 2013 Oct 26. pii: S0968-0896(13)00885-7. doi: 10.1016/j.bmc.2013.10.020. [Epub ahead of print]
Further discovery of caffeic acid derivatives as novel influenza neuraminidase inhibitors.
Xie Y, Huang B, Yu K, Xu W.
Source
Department of Medicinal Chemistry, School of Pharmaceutical Sciences, Shandong University, 44, West Culture Road, Jinan, Shandong 250012, PR China. Electronic address: yuanchaox623@aliyun.com.
Abstract
Eight series of compounds, each series containing two to five compounds were prepared by structural modifications of a lead, which was previously discovered as a mild influenza neuraminidase (NA) inhibitor. On the basis of the biological result, a detailed structure-activity relationship (SAR) was derived and discussed. Several caffeic acid derivatives that acted as non-competitive inhibitors were close or superior to the lead and also presented good antiviral activities in cells. Besides, it was interesting to find that modifications of the lead with different strategies could result in selective inhibition against N1 or N2. The preliminary docking analysis indicated that the 150-cavity of the enzymes played an important role in the selective inhibition.
Copyright ? 2013 Elsevier Ltd. All rights reserved.
KEYWORDS:
Caffeic acid, Influenza, Inhibitor, Neuraminidase
PMID:
24262883
[PubMed - as supplied by publisher]
http://www.ncbi.nlm.nih.gov/pubmed/24262883
Further discovery of caffeic acid derivatives as novel influenza neuraminidase inhibitors.
Xie Y, Huang B, Yu K, Xu W.
Source
Department of Medicinal Chemistry, School of Pharmaceutical Sciences, Shandong University, 44, West Culture Road, Jinan, Shandong 250012, PR China. Electronic address: yuanchaox623@aliyun.com.
Abstract
Eight series of compounds, each series containing two to five compounds were prepared by structural modifications of a lead, which was previously discovered as a mild influenza neuraminidase (NA) inhibitor. On the basis of the biological result, a detailed structure-activity relationship (SAR) was derived and discussed. Several caffeic acid derivatives that acted as non-competitive inhibitors were close or superior to the lead and also presented good antiviral activities in cells. Besides, it was interesting to find that modifications of the lead with different strategies could result in selective inhibition against N1 or N2. The preliminary docking analysis indicated that the 150-cavity of the enzymes played an important role in the selective inhibition.
Copyright ? 2013 Elsevier Ltd. All rights reserved.
KEYWORDS:
Caffeic acid, Influenza, Inhibitor, Neuraminidase
PMID:
24262883
[PubMed - as supplied by publisher]
http://www.ncbi.nlm.nih.gov/pubmed/24262883