RajarshiAayatti MallickGuptabSuranjitaMitraaSukhenduMandalcSwadesh R.Biswasa
DOI: https://doi.org/10.1016/j.virol.2020.10.002
Highlights
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A food grade natural peptide nisin can interact with the human ACE2 receptor.
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For the first time, we unraveled that a commonly used food preservative nisin can block ACE2 receptor.
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Binding affinity of nisin was higher than that of spike protein of SARS-CoV-2 as determined by docking studies.
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It was predicted that nisin competitively binds to the receptor over the spike protein.
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It could be an effective and safest therapeutic against COVID-19 infection.
Abstract
Nisin, a food-grade antimicrobial peptide produced by lactic acid bacteria has been examined for its probable interaction with the human ACE2 (hACE2) receptor, the site where spike protein of SARS-CoV-2 binds. Among the eight nisin variants examined, nisin H, nisin Z, nisin U and nisin A showed a significant binding affinity towards hACE2, higher than that of the RBD (receptor binding domain) of the SARS-CoV-2 spike protein. The molecular interaction of nisin with hACE2 was investigated by homology modeling and docking studies. Further, binding efficiency of the most potent nisin H was evaluated through the interaction of hACE2:nisin H complex with RBD (receptor-binding domain) of SARS-CoV-2 and that of hACE2:RBD complex with nisin H. Here, nisin H acted as a potential competitor of RBD to access the hACE2 receptor. The study unravels for the first time that a globally used food preservative, nisin has the potential to bind to hACE2.
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