Journal
NANOSCALE ADVANCES
Volume 4, Issue 6, Pages -Publisher
ROYAL SOC CHEMISTRY
DOI: 10.1039/d1na00855b
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Funding
- Swedish Research Council (Vetenskapsradet) [2018-03811]
- Swedish Foundation for Strategic Research [ITM17-0218]
- NIH [R21AI146969]
- UAB Research Acceleration Funds
- Swedish Research Council [2018-03811] Funding Source: Swedish Research Council
- Swedish Foundation for Strategic Research (SSF) [ITM17-0218] Funding Source: Swedish Foundation for Strategic Research (SSF)
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This study investigated the interaction between the SARS-CoV-2 nsp1 protein and two types of titania nanoparticles using NMR. The aminoalcohol-capped particles showed strong complexation with a specific part of the protein, potentially interfering with its functionality.
The ongoing world-wide Severe Acute Respiratory Syndrome coronavirus 2 (SARS-CoV-2) pandemic shows the need for new potential sensing and therapeutic means against the CoV viruses. The SARS-CoV-2 nsp1 protein is important, both for replication and pathogenesis, making it an attractive target for intervention. In this study we investigated the interaction of this protein with two types of titania nanoparticles by NMR and discovered that while lactate capped particles essentially did not interact with the protein chain, the aminoalcohol-capped ones showed strong complexation with a distinct part of an ordered alpha-helix fragment. The structure of the forming complex was elucidated based on NMR data and theoretical calculation. To the best of our knowledge, this is the first time that a tailored titanium oxide nanoparticle was shown to interact specifically with a unique site of the full-length SARS-CoV-2 nsp1 protein, possibly interfering with its functionality.
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