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SARS-CoV-2 proteins

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    N-acetyl cysteine: A tool to perturb SARS-CoV-2 spike PROTEIN SARS-CoV-2 spike MESHD protein conformation

    Authors: Utsab Debnath; Amrita Mitra; Varun Dewaker; Yenamandra S. Prabhakar; Raghu Tadala; Kiran Krishnan; Padmakar Wagh; Umashankar Velusamy; Chandru Subramani; Shubhra Agarwal; Sudhanshu Vrati; Aastha Baliyan; Anura V Kurpad; Parthasarathi Bhattacharyya; Amit Mandal

    doi:10.26434/chemrxiv.12687923.v2 Date: 2021-01-06 Source: ChemRxiv

    The infection caused by Severe Acute Respiratory Syndrome Coronavirus 2 MESHD (SARS-CoV-2) resulted in a pandemic with huge death toll and economic consequences. The virus attaches itself to the human epithelial cells through noncovalent bonding of its spike protein PROTEIN with the angiotensin-converting enzyme-2 HGNC ( ACE2 HGNC) receptor on the host cell. We hypothesized that perturbing the functionally active conformation of spike protein PROTEIN through reduction of its solvent accessible disulfide bond, thereby disintegrating its structural architecture, may be a feasible strategy to prevent infection. Proteomics data showed that N-acetyl cysteine ( NAC HGNC), an antioxidant and mucolytic agent been widely in use in clinical medicine, forms covalent conjugates with solvent accessible cysteine residues of spike protein PROTEIN that were disulfide bonded in the native state. In silico analysis indicated that this covalent conjugation perturbed the stereo specific orientations of the interacting key residues of spike protein PROTEIN that resulted in threefold weakening in the binding affinity of spike protein PROTEIN with ACE2 HGNC receptor. Antiviral assay using VeroE6 cells showed that NAC HGNC caused 54.3% inhibition in SARS-CoV-2 replication. Interestingly, almost all SARS-Cov-2 variants conserved cystine residues in the spike protein PROTEIN. Our observed results open avenues for exploring in vivo pharmaco-preventive and therapeutic potential of NAC HGNC for Coronavirus Disease 2019 MESHD ( COVID-19 MESHD).

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MeSH Disease
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