tetano
Editor, Senior Moderator
Carbohydr Res. 2014 Oct 28;402C:152-157. doi: 10.1016/j.carres.2014.10.011. [Epub ahead of print]
[h=1]Anomeric selectivity and influenza A virus inhibition study on methoxylated analogues of Pentagalloylglucose.[/h] Qurat-Ul-Ain S[SUP]1[/SUP], Wang W[SUP]1[/SUP], Yang M[SUP]1[/SUP], Du N[SUP]1[/SUP], Wan S[SUP]1[/SUP], Zhang L[SUP]1[/SUP], Jiang T[SUP]2[/SUP].
[h=3]Author information[/h]
[h=3]Abstract[/h] Anomeric selectivity in galloylation of d-glucose and d-mannose with carboxylic acid was explored under steglich conditions. Base catalyst 4-dimethylaminopyridine favored the formation of alpha-anomers, while adding an acid and carbodiimide favored the formation of beta-anomers. Steric hindrance between α,β-unsaturated acid and C-2 OH stereochemistry (adjacent carbon to anomeric) influenced anomeric selectivity for both d-glucose and d-mannose. The influenza A virus inhibition activities of the synthesized compounds were evaluated in Madin-Darby canine kidney cell line using the cytopathic effect inhibition assay. All the synthetic methoxylated analogues showed more considerable activity against influenza A virus than their corresponding acids, which indicated the sugar core as key functionality for anti-viral activity. The activities of trimethoxy-cinnamic acid Pentagalloylglucose analogues, 3α, 3β, 4α, and 4β (IC[SUB]50,[/SUB] 109.1μM, 134.4μM, 119.5μM, 111.1μM, respectively) were better than those of trimethoxy-benzoic acid Pentagalloylglucose analogues, 1-αβ and 2α, 2β (IC[SUB]50,[/SUB] 209.8μM, 132.9μM, 161.2μM, respectively), which suggested that the double bond in cinnamic acid Pentagalloylglucose analogues makes the major contribution for influenza A virus inhibitory activity. Notably, several anomeric mixtures showed better activities than pure alpha or beta anomer and were almost two times more effective than Ribavirin, a clinically used anti-viral drug.
Copyright ? 2014 Elsevier Ltd. All rights reserved.
[h=4]KEYWORDS:[/h] Anomeric selectivity; Galloylation; Influenza A virus inhibition; Steglich esterification
PMID: 25498015 [PubMed - as supplied by publisher]
http://www.ncbi.nlm.nih.gov/pubmed/25498015
[h=1]Anomeric selectivity and influenza A virus inhibition study on methoxylated analogues of Pentagalloylglucose.[/h] Qurat-Ul-Ain S[SUP]1[/SUP], Wang W[SUP]1[/SUP], Yang M[SUP]1[/SUP], Du N[SUP]1[/SUP], Wan S[SUP]1[/SUP], Zhang L[SUP]1[/SUP], Jiang T[SUP]2[/SUP].
[h=3]Author information[/h]
[h=3]Abstract[/h] Anomeric selectivity in galloylation of d-glucose and d-mannose with carboxylic acid was explored under steglich conditions. Base catalyst 4-dimethylaminopyridine favored the formation of alpha-anomers, while adding an acid and carbodiimide favored the formation of beta-anomers. Steric hindrance between α,β-unsaturated acid and C-2 OH stereochemistry (adjacent carbon to anomeric) influenced anomeric selectivity for both d-glucose and d-mannose. The influenza A virus inhibition activities of the synthesized compounds were evaluated in Madin-Darby canine kidney cell line using the cytopathic effect inhibition assay. All the synthetic methoxylated analogues showed more considerable activity against influenza A virus than their corresponding acids, which indicated the sugar core as key functionality for anti-viral activity. The activities of trimethoxy-cinnamic acid Pentagalloylglucose analogues, 3α, 3β, 4α, and 4β (IC[SUB]50,[/SUB] 109.1μM, 134.4μM, 119.5μM, 111.1μM, respectively) were better than those of trimethoxy-benzoic acid Pentagalloylglucose analogues, 1-αβ and 2α, 2β (IC[SUB]50,[/SUB] 209.8μM, 132.9μM, 161.2μM, respectively), which suggested that the double bond in cinnamic acid Pentagalloylglucose analogues makes the major contribution for influenza A virus inhibitory activity. Notably, several anomeric mixtures showed better activities than pure alpha or beta anomer and were almost two times more effective than Ribavirin, a clinically used anti-viral drug.
Copyright ? 2014 Elsevier Ltd. All rights reserved.
[h=4]KEYWORDS:[/h] Anomeric selectivity; Galloylation; Influenza A virus inhibition; Steglich esterification
PMID: 25498015 [PubMed - as supplied by publisher]
http://www.ncbi.nlm.nih.gov/pubmed/25498015