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Enhanced Inhibition of Influenza A Virus Adhesion by Di- and Trivalent Hemagglutinin Inhibitors

[Image: see text] Multivalent carbohydrate-based ligands were synthesized and evaluated as inhibitors of the adhesion protein HA of the influenza A virus (IAV). HA relies on multivalency for strong viral adhesion. While viral adhesion inhibition by large polymeric molecules has proven viable, limite...

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Autores principales: Lu, Wenjing, Du, Wenjuan, Somovilla, Victor J., Yu, Guangyun, Haksar, Diksha, de Vries, Erik, Boons, Geert-Jan, de Vries, Robert P., de Haan, Cornelis A. M., Pieters, Roland J.
Formato: Online Artículo Texto
Lenguaje:English
Publicado: American Chemical Society 2019
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6627469/
https://www.ncbi.nlm.nih.gov/pubmed/31251606
http://dx.doi.org/10.1021/acs.jmedchem.9b00303
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author Lu, Wenjing
Du, Wenjuan
Somovilla, Victor J.
Yu, Guangyun
Haksar, Diksha
de Vries, Erik
Boons, Geert-Jan
de Vries, Robert P.
de Haan, Cornelis A. M.
Pieters, Roland J.
author_facet Lu, Wenjing
Du, Wenjuan
Somovilla, Victor J.
Yu, Guangyun
Haksar, Diksha
de Vries, Erik
Boons, Geert-Jan
de Vries, Robert P.
de Haan, Cornelis A. M.
Pieters, Roland J.
author_sort Lu, Wenjing
collection PubMed
description [Image: see text] Multivalent carbohydrate-based ligands were synthesized and evaluated as inhibitors of the adhesion protein HA of the influenza A virus (IAV). HA relies on multivalency for strong viral adhesion. While viral adhesion inhibition by large polymeric molecules has proven viable, limited success was reached for smaller multivalent compounds. By linking of sialylated LAcNAc units to di- and trivalent scaffolds, inhibitors were obtained with an up to 428-fold enhanced inhibition in various assays.
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spelling pubmed-66274692019-07-16 Enhanced Inhibition of Influenza A Virus Adhesion by Di- and Trivalent Hemagglutinin Inhibitors Lu, Wenjing Du, Wenjuan Somovilla, Victor J. Yu, Guangyun Haksar, Diksha de Vries, Erik Boons, Geert-Jan de Vries, Robert P. de Haan, Cornelis A. M. Pieters, Roland J. J Med Chem [Image: see text] Multivalent carbohydrate-based ligands were synthesized and evaluated as inhibitors of the adhesion protein HA of the influenza A virus (IAV). HA relies on multivalency for strong viral adhesion. While viral adhesion inhibition by large polymeric molecules has proven viable, limited success was reached for smaller multivalent compounds. By linking of sialylated LAcNAc units to di- and trivalent scaffolds, inhibitors were obtained with an up to 428-fold enhanced inhibition in various assays. American Chemical Society 2019-06-18 2019-07-11 /pmc/articles/PMC6627469/ /pubmed/31251606 http://dx.doi.org/10.1021/acs.jmedchem.9b00303 Text en Copyright © 2019 American Chemical Society This is an open access article published under a Creative Commons Non-Commercial No Derivative Works (CC-BY-NC-ND) Attribution License (http://pubs.acs.org/page/policy/authorchoice_ccbyncnd_termsofuse.html) , which permits copying and redistribution of the article, and creation of adaptations, all for non-commercial purposes.
spellingShingle Lu, Wenjing
Du, Wenjuan
Somovilla, Victor J.
Yu, Guangyun
Haksar, Diksha
de Vries, Erik
Boons, Geert-Jan
de Vries, Robert P.
de Haan, Cornelis A. M.
Pieters, Roland J.
Enhanced Inhibition of Influenza A Virus Adhesion by Di- and Trivalent Hemagglutinin Inhibitors
title Enhanced Inhibition of Influenza A Virus Adhesion by Di- and Trivalent Hemagglutinin Inhibitors
title_full Enhanced Inhibition of Influenza A Virus Adhesion by Di- and Trivalent Hemagglutinin Inhibitors
title_fullStr Enhanced Inhibition of Influenza A Virus Adhesion by Di- and Trivalent Hemagglutinin Inhibitors
title_full_unstemmed Enhanced Inhibition of Influenza A Virus Adhesion by Di- and Trivalent Hemagglutinin Inhibitors
title_short Enhanced Inhibition of Influenza A Virus Adhesion by Di- and Trivalent Hemagglutinin Inhibitors
title_sort enhanced inhibition of influenza a virus adhesion by di- and trivalent hemagglutinin inhibitors
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6627469/
https://www.ncbi.nlm.nih.gov/pubmed/31251606
http://dx.doi.org/10.1021/acs.jmedchem.9b00303
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