PropertyValue
?:abstract
  • To Editor in Chief Chemarxiv /Respected Sir/Madam /Subject : submission of preprint of an article to ChemRxiv on molecular docking studies of arginine and its structural analogues on COV-19 for publication am herewith submitting the preprint of an article entitled “ Binding ability studies of arginine, citrulline, N-acetyl citrulline and thiocitrulline with SARS Cov-2 main protease using molecular docking studies ” for publication as preprint in “ChemRxiv” In this paper the binding abilities of arginine, citrulline, N-acetyl citrulline and thiocitrulline with SARS-COV-2 protease have been examined using molecular docking studies The ligands used for docking has moderate binding affinity to active sites of main protease in terms of values The binding affinities of these ligands are in the range of -3 1 to -5 1 kcal mol su-1 /su All the ligands bind selectively to Cys-145 and also to other amino acids surrounding to it in the main protease Of which arginine forms less number of weaker bonds compared to the other ligands, it by itself is a precursor for the formation of citrulline analogues with in the cell Major advantage of using the above ligands is that in addition to its preferential binding these molecules also have the ability to enhance the immunity of the cells by the generation of nitric oxide in presence of enzymes thereby protecting them Our results show that N-acetyl citrulline, citrulline, thiocitrulline and arginine may be used as a supplement during the treatment of SARS-COV-2 request your good self to kindly accept the article and get it published as pre-print in your esteemed ChemRxiv Thanking you /With regards /Ramesh T N (adityaramesh77@yahoo com)
is ?:annotates of
?:creator
?:license
  • unk
?:publication_isRelatedTo_Disease
?:source
  • WHO
?:title
  • Binding Ability Studies of Arginine, Citrulline, N-Acetyl Citrulline and Thiocitrulline with SARS Cov-2 Main Protease Using Molecular Docking Studies
?:type
?:who_covidence_id
  • #319
?:year
  • 2020

Metadata

Anon_0  
expand all