Submission Details
Molecule(s):
CC(CNC(=O)C(C)Cc1c[nH]c2ccccc12)Cc1ccccc1
O=C(Cc1c[nH]c2ccccc12)Nc1ccccc1
Design Rationale:
Both of these are non-covalent inhibitors that combine the characteristics of many of the most common non-covalent hits found for the COV-2 protease enzyme. They also fulfill the Lipinski's rule of 5. Each structure contains a ring on one end that mimics the tryptophan ring from fragment 1093, this ring resides in the pocket right above the cysteine of the active site The other end of the two structures contain a phenyl ring which resembles many of the noncovalent inhibitors, this phenyl ring resides in the pocket right by the cysteine(not above) Theses two inhibitors may be able to form the noncovalent interactions that can tighten up the pocket of the enzyme active site
Other Notes:
These inhibitors were inspired by previous noncovalent inhibitors that reside in the pocket of the enzyme