Enzyme-Based Antiviral Potential of Cinnamomum verum J. Presl. Essential Oil and Its Major Component (E)-Cinnamaldehyde

Abstract

In the present study, Cinnamomum verum J. Presl. bark essential oil and its main component cinnamaldehyde was evaluated in vitro for neuraminidase (NA), transmembrane serine protease (TMPRSS2), and angiotensin converting enzyme 2 (ACE2) inhibitory activities. The chemical composition of C. verum essential oil was confirmed by both gas chromatography-mass spectrometry (GC/MS), and gas chromatography-flame ionization detection (GC-FID), where 75.9% (E)-cinnamaldehyde was the major component. The ACE2, NA, and TMPRSS2 enzyme inhibitions of C. verum bark essential oil at 20 μg/mL concentration, and (E)-cinnamaldehyde (5 μg/mL) were calculated and compared in the range of 54.2-89.9%. Molecular docking results supported that (E)-cinnam-aldehyde was specific to ACE2 with 89.9% inhibition. Our findings suggest further in vivo studies to confirm the effective and safe use of the essential oil as well as the (E)-cinnamaldehyde.

Figure 1

(a) Cinnamaldehyde prefers to bind in the S1 site of ACE2 subdomain II. The zinc center located in subdomain I can be seen in the background. Black dotted lines represent hydrogen bonds. (b) The binding mode of cinnamaldehyde for neuraminidase features substrate-like bidentate hydrogen bonding with Arg 118. To some extent, the binding also is similar to that of oseltamivir. (c) Hydrophobic interaction of cinnamaldehyde with Gln 438 in the S3 subsite of TMPRSS2 away from the catalytic triad: Ser 441, His 296, and Asp 345.