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. 2023 Feb 22;15(7):9058-9065.
doi: 10.1021/acsami.2c21187. Epub 2023 Feb 14.

Surface-Functionalized Metal-Organic Frameworks for Binding Coronavirus Proteins

Aamod V Desai  1 , Simon M Vornholt  1 , Louise L Major  2 , Romy Ettlinger  1 , Christian Jansen  3 , Daniel N Rainer  1 , Richard de Rome  1 , Venus So  1 , Paul S Wheatley  1 , Ailsa K Edward  1 , Caroline G Elliott  1 , Atin Pramanik  1 , Avishek Karmakar  4 , A Robert Armstrong  1 , Christoph Janiak  3 , Terry K Smith  1   2 , Russell E Morris  1
Affiliations

Surface-Functionalized Metal-Organic Frameworks for Binding Coronavirus Proteins

Aamod V Desai et al. ACS Appl Mater Interfaces. .

Abstract

Since the outbreak of SARS-CoV-2, a multitude of strategies have been explored for the means of protection and shielding against virus particles: filtration equipment (PPE) has been widely used in daily life. In this work, we explore another approach in the form of deactivating coronavirus particles through selective binding onto the surface of metal-organic frameworks (MOFs) to further the fight against the transmission of respiratory viruses. MOFs are attractive materials in this regard, as their rich pore and surface chemistry can easily be modified on demand. The surfaces of three MOFs, UiO-66(Zr), UiO-66-NH2(Zr), and UiO-66-NO2(Zr), have been functionalized with repurposed antiviral agents, namely, folic acid, nystatin, and tenofovir, to enable specific interactions with the external spike protein of the SARS virus. Protein binding studies revealed that this surface modification significantly improved the binding affinity toward glycosylated and non-glycosylated proteins for all three MOFs. Additionally, the pores for the surface-functionalized MOFs can adsorb water, making them suitable for locally dehydrating microbial aerosols. Our findings highlight the immense potential of MOFs in deactivating respiratory coronaviruses to be better equipped to fight future pandemics.

Keywords: SARS-CoV-2; antiviral drugs; metal−organic framework; protein binding; water adsorption.

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Conflict of interest statement

The authors declare the following competing financial interest(s): Aamod V. Desai, Romy Ettlinger, Russell E. Morris (University of St Andrews). UK Patent Application, 2022.

Figures

Scheme 1
Scheme 1. Schematic Representation of the Utilization of Different MOFs, Namely, UiO-66-X (X = −H, NH2, NO2), with Hydrophilic Pores for Dehydrating Aerosols/Droplets and Different Surface Functionalization for Immobilizing Viruses, i.e., Folic Acid, Nystatin, and Tenofovir with the Expected Binding Groups to the MOF Surface Highlighted in Blue
Figure 1
Figure 1
Characterization for surface-modified UiO-66-NO2—(a) PXRD patterns, (b) TGA profiles (for a better comparison of their decomposition profiles, the release of different amounts of water due to their respective water adsorption behaviors below 100 °C was omitted), and (c) water adsorption isotherms recorded at 298 K. Photographs and SEM micrographs of (d) UiO-66-NO2, (e) UiO-66-NO2-FA, (f) UiO-66-NO2-Nys, and (g) UiO-66-NO2-Teno; scale bar = 500 nm (color code for plots: UiO-66-NO2—gray, UiO-66-NO2-FA—red, UiO-66-NO2-Nys—blue, UiO-66-NO2-Teno—green).
Figure 2
Figure 2
(a) Amount of BSA protein binding (%) when treated with 6 μg of BSA in aqueous solution. (b) Comparison of protein binding (%) of UiO-66-NO2 and its derivatives (UiO-66-NO2-FA and UiO-66-NO2-Teno) upon treatment with 60 μg of BSA, Annexin-g03104, and recombinant S-protein of SARS in water (plots are an average value of triplicate measurements, error bars represent standard deviation).
Figure 3
Figure 3
TEM micrographs of bovine serum albumin (BSA; (a, d)), as well as pristine UiO-66-NO2 (b, e) and UiO-66-NO2-FA (c, f) after the BSA protein binding experiment. Scale bar: (a–c) 200 nm and (d–f) 100 nm.
See this image and copyright information in PMC

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