Iterative Optimization and Structure–Activity Relationship Studies of Oseltamivir Amino Derivatives as Potent and Selective Neuraminidase Inhibitors via Targeting 150-Cavity

Journal of Medicinal Chemistry
2022.0

Abstract

With our continuous endeavors in seeking neuraminidase (NA) inhibitors, we reported herein three series of novel oseltamivir amino derivatives with the goal of exploring the druggable chemical space inside the 150-cavity of influenza virus NAs. Among them, around half of the compounds in <b>series C</b> were demonstrated to be better inhibitors against both wild-type and oseltamivir-resistant group-1 NAs than oseltamivir carboxylate (OSC). Notably, compounds <b>12d</b>, <b>12e</b>, <b>15e</b>, and <b>15i</b> showed more potent or equipotent antiviral activity against H1N1, H5N1, and H5N8 viruses compared to OSC in cellular assays. Furthermore, compounds <b>12e</b> and <b>15e</b> exhibited high metabolic stability in human liver microsomes (HLMs) and low inhibitory effect on main cytochrome P450 (CYP) enzymes, as well as low acute/subacute toxicity and certain antiviral efficacy <i>in vivo</i>. Also, pharmacokinetic (PK) and molecular docking studies were performed. Overall, <b>12e</b> and <b>15e</b> possess great potential to serve as anti-influenza candidates and are worthy of further investigation.

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