TY - JOUR
T1 - Carotane sesquiterpenes fromFerula vesceritensis:in silicoanalysis as SARS-CoV-2 binding inhibitors
AU - Mohamed, Tarik A.
AU - Elshamy, Abdelsamed I.
AU - Ibrahim, Mahmoud A.A.
AU - Zellagui, Ammar
AU - Moustafa, Mahmoud F.
AU - Abdelrahman, Alaa H.M.
AU - Ohta, Shinji
AU - Pare, Paul W.
AU - Hegazy, Mohamed Elamir F.
N1 - Publisher Copyright:
© The Royal Society of Chemistry 2020.
PY - 2020/9/18
Y1 - 2020/9/18
N2 - Two sesquiterpenes, 8α-anisate-dauc-4-ene-3,9-dione (webiol anisate) (1) and 10α-acetoxy-6α-benzoate-jaeschkeanadiol (2) as well as, ten known analogues (3-10), and two sesquiterpene coumarins (11-12) were isolated from an organic root extract ofFerula vesceritensis(Fam. Apiaceae). Chemical structures were elucidated based on IR, 1D- and 2D-NMR and HRMS, spectroscopic analyses. With molecular overlap observed between two protease inhibitors that are being examined as anti-COVID-19 drugs, and sesquiterpenes isolated here, metabolite molecular docking calculations were made using the main protease (Mpro), which is required for viral multiplication as well as RNA-dependent RNA polymerase (RdRp).In silicobinding-inhibition analysis predicted that selectF. vesceritensissesquiterpenes can bind to these enzymes required for viral replication. Structures of the isolated constituents were also consistent with the chemo-systematic grouping ofF. vesceritensissecondary metabolites with otherFerulaspecies.
AB - Two sesquiterpenes, 8α-anisate-dauc-4-ene-3,9-dione (webiol anisate) (1) and 10α-acetoxy-6α-benzoate-jaeschkeanadiol (2) as well as, ten known analogues (3-10), and two sesquiterpene coumarins (11-12) were isolated from an organic root extract ofFerula vesceritensis(Fam. Apiaceae). Chemical structures were elucidated based on IR, 1D- and 2D-NMR and HRMS, spectroscopic analyses. With molecular overlap observed between two protease inhibitors that are being examined as anti-COVID-19 drugs, and sesquiterpenes isolated here, metabolite molecular docking calculations were made using the main protease (Mpro), which is required for viral multiplication as well as RNA-dependent RNA polymerase (RdRp).In silicobinding-inhibition analysis predicted that selectF. vesceritensissesquiterpenes can bind to these enzymes required for viral replication. Structures of the isolated constituents were also consistent with the chemo-systematic grouping ofF. vesceritensissecondary metabolites with otherFerulaspecies.
UR - http://www.scopus.com/inward/record.url?scp=85092247029&partnerID=8YFLogxK
U2 - 10.1039/d0ra06901a
DO - 10.1039/d0ra06901a
M3 - Article
AN - SCOPUS:85092247029
SN - 2046-2069
VL - 10
SP - 34541
EP - 34548
JO - RSC Advances
JF - RSC Advances
IS - 57
ER -