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  Fucose-functionalized precision glycomacromolecules targeting human norovirus capsid protein

Bücher, K. S., Yan, H., Creutznacher, R., Ruoff, K., Mallagaray, A., Grafmüller, A., et al. (2018). Fucose-functionalized precision glycomacromolecules targeting human norovirus capsid protein. Macromolecules, 19(9), 3714-3724. doi:10.1021/acs.biomac.8b00829.

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 Urheber:
Bücher, Katharina Susanne, Autor
Yan, Hao, Autor
Creutznacher, Robert, Autor
Ruoff, Kerstin, Autor
Mallagaray, Alvaro, Autor
Grafmüller, Andrea1, Autor           
Dirks, Jan Sebastian, Autor
Kilic, Turgay, Autor
Weickert, Sabrina, Autor
Rubailo, Anna, Autor
Drescher, Malte, Autor
Schmidt, Stephan, Autor
Hansman, Grant, Autor
Peters, Thomas, Autor
Uetrecht, Charlotte, Autor
Hartmann, Laura, Autor
Affiliations:
1Andrea Grafmüller, Theorie & Bio-Systeme, Max Planck Institute of Colloids and Interfaces, Max Planck Society, ou_1863323              

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 Zusammenfassung: Norovirus infection is the major cause of non-bacterial gastroenteritis in humans and has been the subject of numerous studies investigating the virus’s biophysical properties and biochemical function with the aim of deriving novel and highly potent entry inhibitors to prevent infection. Recently, it has been shown that the protruding P domain dimer (P-dimer) of a GII.10 Norovirus strain exhibits two new binding sites for L-fucose in addition to the canonical binding sites. Thus these sites provide a novel target for the design of multivalent fucose ligands as entry inhibitors of norovirus infections. In this current study, a first generation of multivalent fucose-functionalized glycomacromolecules was synthesized and applied as model structures to investigate the potential targeting of fucose binding sites in human norovirus P-dimer. Following previously established solid phase polymer synthesis, eight precision glycomacromolecules varying in number and position of fucose ligands along an oligo(amidoamine) backbone were obtained and then used in a series of binding studies applying native MS, NMR and X-ray crystallography. We observed only one fucose per glycomacromolecule binding to one P-dimer resulting in similar binding affinities for all fucose-functionalized glycomacromolecules, which based on our current findings we attribute to the overall size of macromolecular ligands and possibly to steric hindrance.

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 Datum: 2018-08-022018
 Publikationsstatus: Erschienen
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 Art der Begutachtung: Expertenbegutachtung
 Identifikatoren: DOI: 10.1021/acs.biomac.8b00829
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Titel: Macromolecules
Genre der Quelle: Zeitschrift
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Ort, Verlag, Ausgabe: Washington, D.C. : American Chemical Society
Seiten: - Band / Heft: 19 (9) Artikelnummer: - Start- / Endseite: 3714 - 3724 Identifikator: ISSN: 0024-9297