BioAcyl Corp
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Nie, C., Sahoo, A. K., Herrmann, A., & others. (2022). Charge matters: Mutations in omicron variant favor binding to cells. Circ. Res. n/a(n/a). Added by: Dr. Enrique Feoli (17/01/2022, 12:22) Last edited by: Dr. Enrique Feoli (17/01/2022, 12:25) |
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| Resource type: Journal Article DOI: 10.1002/cbic.202100681 ID no. (ISBN etc.): 1439-4227 BibTeX citation key: Nie2022 View all bibliographic details  |
Categories: BioAcyl Corp Subcategories: Polysulfate polianions Creators: Herrmann, Nie, others, Sahoo Collection: Circ. Res. |
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| Abstract |
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Evidence is strengthening 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 a chemical rational 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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