Scientists have discovered a new vulnerability in a novel coronavirus spike protein that allows the virus to enter host cells. COVID-19 (new coronavirus infectious disease) (# If there is no character limit, add brackets when first appearing..
Researchers, including researchers at Northwestern University in the United States, point out that spike proteins contain viral binding sites that attach to host cells and allow them to infect the body. .. A study presented at ACS Nano used simulations of this protein on a microscale on the order of nanometers, with positively charged sites (called polybasic cleavage sites) 10 nanometers away from the actual bond. I found a site of spike protein. They state that this positively charged site allows strong binding between the spike protein of the novel coronavirus SARS-CoV-2 and the negatively charged human cell receptor.
Using this discovery, scientists then designed a negatively charged molecule that binds to a positively charged cleavage site. They said that blocking this site would prevent the virus from binding to host cells.
“Our research shows that blocking this cleavage site may serve as a viable prophylactic treatment that reduces the ability of the virus to infect humans.” “Our results are: “It describes an study showing that mutations in the SARS-CoV-2 spike protein affected viral infectivity,” she said. It consists of protein building blocks, amino acid molecules, and a novel coronavirus polybasic cleavage site that has remained elusive since the outbreak of COVID-19, he said. Previous studies have shown that these sites are essential for virus virulence and transmission. In the current study, Olvera de la Cruz and his team found that the polybasic cleavage site is 10 nanometers from the human cell receptor. This is a discovery that has brought unexpected insights.
Baofu Qiao, lead author of research at Northwestern University, said: “Under physiological conditions, all electrostatic interactions no longer occur at distances greater than 1 nanometer,” Qiao said.
“The function of the polybasic cleavage site remains elusive,” Olvera de la Cruz said. “But it seems to be cleaved by an enzyme (furin) that is abundant in the lungs, suggesting that the cleavage site is important for the virus’ entry into human cells,” she added.
Scientists are then planning to work with chemists and pharmacologists to design new drugs that may bind to spike proteins.
(This article has been published from the telegraph agency feed with no changes to the text. Only the headings have changed.)
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