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  Charge matters : mutations in Omicron variant favor binding to cells

Nie, C., Sahoo, A. K., Netz, R. R., Herrmann, A., Ballauff, M., & Haag, R. (2022). Charge matters: mutations in Omicron variant favor binding to cells. Chembiochem, 23(6): e202100681. doi:10.1002/cbic.202100681.

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Nie, Chuanxiong, Author
Sahoo, Anil Kumar1, Author           
Netz, Roland R., Author
Herrmann, Andreas, Author
Ballauff, Matthias, Author
Haag, Rainer, Author
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1Richard Weinkamer, Biomaterialien, Max Planck Institute of Colloids and Interfaces, Max Planck Society, ou_1863295              

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 Abstract: Evidence is strengthening to suggest that the novel SARS-CoV-2 mutant Omicron, with its more than 60 mutations, will spread and dominate worldwide. Although the mutations in the spike protein are known, the molecular basis for why the additional mutations in the spike protein that have not previously occurred account for Omicron's higher infection potential, is not understood. We propose, based on chemical rational and molecular dynamics simulations, that the elevated occurrence of positively charged amino acids in certain domains of the spike protein (Delta: +4; Omicron: +5 vs. wild type) increases binding to cellular polyanionic receptors, such as heparan sulfate due to multivalent charge-charge interactions. This observation is a starting point for targeted drug development.

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Language(s): eng - English
 Dates: 2022-01-122022
 Publication Status: Published in print
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 Identifiers: DOI: 10.1002/cbic.202100681
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Title: Chembiochem
  Other : Chembiochem
Source Genre: Journal
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Publ. Info: Weinheim, Germany : Wiley-VCH
Pages: - Volume / Issue: 23 (6) Sequence Number: e202100681 Start / End Page: - Identifier: ISSN: 1439-4227