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10.1016/j.saa.2021.120595 http://scihub22266oqcxt.onion/10.1016/j.saa.2021.120595 34815178!8591854!34815178     free     free     free Deprecated: Implicit conversion from float 213.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 213.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 213.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 213.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 213.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534       Spectrochim+Acta+A+Mol+Biomol+Spectrosc 2022 ; 267 (Pt 2): 120595 Nephropedia Template TP {{tp|p=34815178|t=2022. Heparin interacts with the main protease of SARS-CoV-2 and inhibits its activity |pdf=|usr=}}{{34815178}} gab.com Text Heparin interacts with the main protease of SARS-CoV-2 and inhibits its activity JO: Spectrochim Acta A Mol Biomol Spectrosc http://www.kidney.de/pget.php?&tw=1&pmid=34815178 #FOAvip The ability of SARS-CoV-2 to replicate in host cells is dependent on its main protease (M(pro), also called 3CLpro) that cut the viral precursor polyproteins and is a major target for antiviral drug design. Here, we showed that heparin interacts with the M(pro) of SARS-CoV-2 and inhibits its activity. Protein fluorescence quenching showed that heparin strongly binds to the M(pro) protein with dissociation constants K(D) of 16.66 and 31.60 muM at 25 and 35 degrees C, respectively. From thermodynamic parameters of the interaction, there are hydrophobic and hydrogen bond interactions between them. Fluorescence resonance energy transfer (FRET) assay demonstrated that heparin inhibits the proteolytic activity of M(pro) with an inhibition constant Ki of 6.9 nM and a half maximal inhibitory concentrations (IC(50)) of 7.8 +/- 2.6 nM. Furthermore, molecular docking analysis revealed that the recognition and binding groups of heparin within the active site of SARS-CoV-2 M(pro) provide important new information for the characteristics of the interactions of heparin with the protease. Our finding suggested that heparin might have a potential role in inhibiting SARS-CoV-2 infection through inhibiting M(pro) activity of SARS-CoV-2. Twit Text FOAVip Heparin interacts with the main protease of SARS-CoV-2 and inhibits its activity ????Spectrochim Acta A Mol Biomol Spectrosc http://www.kidney.de/pget.php?&tw=1&pmid=34815178 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=34815178 #FOAvip English Wikipedia <ref>{{Cite pmid|34815178}}</ref> Heparin interacts with the main protease of SARS-CoV-2 and inhibits its activity #MMPMID34815178 Li J; Zhang Y; Pang H; Li SJ Spectrochim Acta A Mol Biomol Spectrosc 2022[Feb]; 267 (Pt 2): 120595 PMID34815178show ga The ability of SARS-CoV-2 to replicate in host cells is dependent on its main protease (M(pro), also called 3CLpro) that cut the viral precursor polyproteins and is a major target for antiviral drug design. Here, we showed that heparin interacts with the M(pro) of SARS-CoV-2 and inhibits its activity. Protein fluorescence quenching showed that heparin strongly binds to the M(pro) protein with dissociation constants K(D) of 16.66 and 31.60 muM at 25 and 35 degrees C, respectively. From thermodynamic parameters of the interaction, there are hydrophobic and hydrogen bond interactions between them. Fluorescence resonance energy transfer (FRET) assay demonstrated that heparin inhibits the proteolytic activity of M(pro) with an inhibition constant Ki of 6.9 nM and a half maximal inhibitory concentrations (IC(50)) of 7.8 +/- 2.6 nM. Furthermore, molecular docking analysis revealed that the recognition and binding groups of heparin within the active site of SARS-CoV-2 M(pro) provide important new information for the characteristics of the interactions of heparin with the protease. Our finding suggested that heparin might have a potential role in inhibiting SARS-CoV-2 infection through inhibiting M(pro) activity of SARS-CoV-2. |*COVID-19[MESH] |*SARS-CoV-2[MESH] |Antiviral Agents[MESH] |Heparin[MESH] |Humans[MESH] |Molecular Docking Simulation[MESH] |Peptide Hydrolases[MESH]Heparin interacts with the main protease of SARS-CoV-2 and inhibits it(epmc).pdf DeepDyve Pubget Overpricing