id	author	title	date	pages	extension	mime	words	sentences	flesch	summary	cache	txt
cord-103085-vf4qyvft	Seitz, Christian	Multiscale simulations examining glycan shield effects on drug binding to influenza neuraminidase	2020-11-02		.txt	text/plain	9735	512	50	Using Brownian dynamics simulations, we observe a twoto eight-fold decrease in the rate of ligand binding to the primary binding site of neuraminidase due to the presence of glycans. We have utilized BD to estimate the rates of binding of small molecules to the primary (i.e. active/catalytic) and secondary (i.e. hemadsorption) binding sites of influenza neuraminidase in glycosylated and unglycosylated states. The protein-ligand atom pairs were taken from crystal structures of ligands in the primary and secondary sites of neuraminidase for each monomer, and simulations were run for the full tetramer. Keeping in mind the primary and secondary binding sites are located just beneath the glycans (Figure 1) , the size and flexibility of the glycans here shows that they have the capability to "shield" the binding sites from ligand association. (A) The glycan structures from the MD simulations show a moderate association rate inhibition to the primary binding site irrespective of ligand chosen.	./cache/cord-103085-vf4qyvft.txt	./txt/cord-103085-vf4qyvft.txt