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Heteromultivalent Ligand Display on Reversible Self-Assembled Monolayers (rSAMs): A Fluidic Platform for Tunable Influenza Virus Recognition
Malmö University, Faculty of Health and Society (HS), Department of Biomedical Science (BMV). Malmö University, Biofilms Research Center for Biointerfaces.
Malmö University, Faculty of Health and Society (HS), Department of Biomedical Science (BMV). Malmö University, Biofilms Research Center for Biointerfaces.
Malmö University, Faculty of Health and Society (HS), Department of Biomedical Science (BMV). Malmö University, Biofilms Research Center for Biointerfaces.ORCID iD: 0000-0002-2392-3305
2024 (English)In: ACS Applied Materials and Interfaces, ISSN 1944-8244, E-ISSN 1944-8252, Vol. 16, no 3, p. 3139-3146Article in journal (Refereed) Published
Abstract [en]

We report on the design of heteromultivalent influenza A virus (IAV) receptors based on reversible self-assembled monolayers (SAMs) featuring two distinct mobile ligands. The principal layer building blocks consist of α-(4-amidinophenoxy)alkanes decorated at the ω-position with sialic acid (SA) and the neuraminidase inhibitor Zanamivir (Zan), acting as two mobile ligands binding to the complementary receptors hemagglutinin (HA) and neuraminidase (NA) on the virus surface. From ternary amphiphile mixtures comprising these ligands, the amidines spontaneously self-assemble on top of carboxylic acid-terminated SAMs to form reversible mixed monolayers (rSAMs) that are easily tunable with respect to the ligand ratio. We show that this results in the ability to construct surfaces featuring a very strong affinity for the surface proteins and specific virus subtypes. Hence, an rSAM prepared from solutions containing 15% SA and 10% Zan showed an exceptionally high affinity and selectivity for the avian IAV H7N9 (Kd = 11 fM) that strongly exceeded the affinity for other subtypes (H3N2, H5N1, H1N1). Changing the SA/Zan ratio resulted in changes in the relative preference between the four tested subtypes, suggesting this to be a key parameter for rapid adjustments of both virus affinity and selectivity.

Place, publisher, year, edition, pages
American Chemical Society (ACS), 2024. Vol. 16, no 3, p. 3139-3146
Keywords [en]
H5N1, H7N9, IAV subtype selectivity, virus monitoring, virus recognition
National Category
Biomaterials Science
Identifiers
URN: urn:nbn:se:mau:diva-65698DOI: 10.1021/acsami.3c15699ISI: 001150615700001PubMedID: 38197122Scopus ID: 2-s2.0-85182563097OAI: oai:DiVA.org:mau-65698DiVA, id: diva2:1834269
Available from: 2024-02-02 Created: 2024-02-02 Last updated: 2024-02-27Bibliographically approved

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Sergeeva, YuliaYeung, Sing YeeSellergren, Börje

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