Surface-Functionalized Metal-Organic Frameworks for Binding Coronavirus Proteins

Aamod Vikas Desai*, Simon M. Vornholt, Louise L Major, Romy Ettlinger, Christian Jansen, Daniel Rainer, Richard de Rome, Venus So, Paul S. Wheatley, Ailsa K. Edward, Caroline Elliott, Atin Pramanik, Avishek Karmakar, Robert Armstrong, Christoph Janiak, Terry K Smith, Russell Edward Morris

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

9 Citations (Scopus)
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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.
Original languageEnglish
Pages (from-to)9058–9065
Number of pages8
JournalACS Applied Materials & Interfaces
Issue number7
Early online date14 Feb 2023
Publication statusPublished - 22 Feb 2023


  • SARS-CoV-2
  • Antiviral drugs
  • Metal-organic framework
  • Protein binding
  • Water adsorption


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