id	author	title	date	pages	extension	mime	words	sentences	flesch	summary	cache	txt
cord-274280-x5s4l0pp	Yang, Jinsung	Molecular interaction and inhibition of SARS-CoV-2 binding to the ACE2 receptor	2020-09-11		.txt	text/plain	7278	403	56	Here, we analyze the biophysical properties of the SARS-CoV-2 S-glycoprotein binding, on model surfaces and on living cells, to ACE2 receptors using force-distance (FD) curve-based atomic force microscopy (FD-curve-based AFM) (Fig. 1c) . used FD-curve-based AFM to evaluate at the single-molecule level the binding strength of the interaction established between the glycosylated S1 subunit and ACE2 receptors on model surfaces (Fig. 2a) . To investigate the properties of the binding complex, force-distance (FD) curves were recorded by repeatedly approaching and withdrawing the S1 subunit or RBD-functionalized tip from the ACE2 model surface (Fig. 2a, b) . To this end, we synthetized four different peptides (sequences provided in Supplementary Fig. 9 ), which have been selected to mimic the regions of ACE2 that interact with the S1 subunit as determined by the crystal structure 29 , and we tested their binding inhibition properties using our single-molecule force spectroscopy approach (Fig. 4a, b) .	./cache/cord-274280-x5s4l0pp.txt	./txt/cord-274280-x5s4l0pp.txt