Reduction of hemagglutination induced by a SARS-CoV-2 spike protein fragment using an amyloid-binding benzothiazole amphiphile.

Autor: Li M; Department of Chemistry and Biochemistry, University of California, San Diego, 9500 Gilman Drive, La Jolla, 92093-0358, USA., Castro Lingl S; Department of Chemistry and Biochemistry, University of California, San Diego, 9500 Gilman Drive, La Jolla, 92093-0358, USA., Yang J; Department of Chemistry and Biochemistry, University of California, San Diego, 9500 Gilman Drive, La Jolla, 92093-0358, USA. jerryyang@ucsd.edu.
Jazyk: angličtina
Zdroj: Scientific reports [Sci Rep] 2024 May 29; Vol. 14 (1), pp. 12317. Date of Electronic Publication: 2024 May 29.
DOI: 10.1038/s41598-024-59585-4
Abstrakt: COVID-19 infection is associated with a variety of vascular occlusive morbidities. However, a comprehensive understanding of how this virus can induce vascular complications remains lacking. Here, we show that a peptide fragment of SARS-CoV-2 spike protein, S192 (sequence 192-211), is capable of forming amyloid-like aggregates that can induce agglutination of red blood cells, which was not observed with low- and non-aggregated S192 peptide. We subsequently screened eight amyloid-binding molecules and identified BAM1-EG 6 , a benzothiazole amphiphile, as a promising candidate capable of binding to aggregated S192 and partially inhibiting its agglutination activity. These results provide new insight into a potential molecular mechanism for the capability of spike protein metabolites to contribute to COVID-19-related blood complications and suggest a new therapeutic approach for combating microvascular morbidities in COVID-19 patients.
(© 2024. The Author(s).)
Databáze: MEDLINE
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