id	author	title	date	pages	extension	mime	words	sentences	flesch	summary	cache	txt
cord-308583-vtmwv8zl	Du, Qishi	Molecular modeling and chemical modification for finding peptide inhibitor against severe acute respiratory syndrome coronavirus main proteinase	2005-02-15		.txt	text/plain	3856	225	63	In this research we study the cleavage mechanism, the properties of the relevant chemical bonds, and the catalytic interactions between the octapeptides and the SARS CoV M pro using molecular mechanical and quantum chemical simulations to provide useful insights for the chemical modification. The docking calculation between SARS CoV M pro and the octapeptide AVLQSGFR was performed using the molecular although still bound to the active site, the peptide has lost its cleavability after its scissile bond was modified from a hybrid peptide bond to a strong bond. Fig. 5B is the contour map of differential electronic density of the peptide bond Gln-Ser in the octapeptide AVLQSGFR, obtained by subtracting the electron density in the gaseous phase from the electron density in the background [23] of SARS CoV M pro and solvent water molecules. For the peptide inhibitor of proteinase, the chemical modification to cleavable octapeptide should focus on the scissile peptide bond between R 1 and R 1 0 to be cleaved by SARS CoV M pro .	./cache/cord-308583-vtmwv8zl.txt	./txt/cord-308583-vtmwv8zl.txt