In silico studies revealed LDN interacts with the
receptor-binding motif of SARS-CoV-2 -RBD
The latest research shows that the spike-receptor binding domain (RBD)
sequence of SARS-CoV-2 interacts with host receptor ACE2 and this
RBD-ACE2 complex plays a key role in virus invasion and virulence. Based
on the current research progress, the RBD-ACE2 complex is considered as
a target for the treatment of coronavirus infection to block SARS-CoV-2
from entering host cells.
To understand the mode of interaction naltrexone in the binding
interface of RBD-ACE2 complex, molecular docking was performed using
AutoDock. The docking scores of the top ten complexes have been
summarized in Table S1 . As evidenced by the top-ranked
conformation (as shown in Figure 2 ), the naltrexone prefers to
bind in the cavity formed RBD and ACE2 receptor. Tyr505 and Glu406 of
RBD formed two crucial hydrogen bonds with the naltrexone with an atomic
distance of 2.08 and 1.80, while, Arg403 formed electrostatic contact.
While the His34, Glu37, and Phe390 of ACE2 displayed several hydrophobic
contacts (mostly pi-alkyl contacts) with naltrexone.