Angiotensin-Converting Enzyme 2 (ACE2) of marine biota: a preliminary study of potential therapy for SARS-CoV-2 infection

Abstract

A new coronavirus, SARS-CoV-2, is responsible for the current pandemic causing severe respiratory disease. It has been known that the receptor for SARS-CoV-2 entry into the host cell is the angiotensin-converting enzyme 2 (ACE2). This receptor is expressed in a wide array of organs, for example, the kidneys and gastrointestinal tract, but rarely present in the circulation. The soluble form of ACE2 proposed as a potential therapy for SARS-CoV-2 infection. This research aimed to explore angiotensin-converting enzyme 2 (ACE2) from marine biota as the source of ACE2, which is potential for the therapy of SARS-CoV-2 infection. This explorative study was conducted by retrieving the angiotensin-converting enzyme 2 (ACE2) from the database of protein (UniProt). The samples of the study were ACE2 of marine vertebrate, namely Delphinapterus leucas and ACE2 of marine invertebrate, namely Protunus trituberculatus. 3-D structures of ACE2 proteins unavailable in the protein database were modeled in Swiss Model. Molecular docking was conducted by using ClusPro.2.2. The data were analyzed descriptively. The molecular docking results revealed that the binding energy of spike glycoprotein of SARS-CoV-2 and human ACE2 was -988.5 kcal/mol. The binding energy of spike glycoprotein of SARS-CoV-2 and Delphinapterus leucas (Beluga whale) ACE2 was -946.4 kcal/mol. Meanwhile, the binding energy of spike glycoprotein of SARS-CoV-2 and Protunus trituberculatus (swimming crabs) ACE2 was -778.4 kcal/mol. The binding energy of spike glycoprotein of SARS-CoV-2 and Delphinapterus leucas (Beluga whale) ACE2 was closed to the binding energy of spike glycoprotein of SARS-CoV-2 and human ACE2. Hence, ACE2 of Delphinapterus leucas has the potential to be used as a therapeutic candidate from marine biota to suppress the SARS-CoV-2 transmission.

Online teaching and its impact on self-monitoring of faculty members: learnings for the future from a pandemic

“…Previous studies look at the challenges faced by teachers during the pandemic in the different dimensions pertaining to specific subjects (Sugianto and Ulfah, 2020; Gurung, 2021; Hermansyah and Aridah, 2021; Barrow et al. , 2021; Borba, 2021; Ambawati et al. , 2021) in distinct geographical contexts like Israel, England, China, Portugal (Donitsa-Schmidt and Ramot, 2020; La Velle et al.…”

Marine-Derived Bioactive Metabolites as a Potential Therapeutic Intervention in Managing Viral Diseases: Insights from the SARS-CoV-2 In Silico and Pre-Clinical Studies

“…For instance, ACE2 ( 234 ) of Delphinapterus leucas (Beluga whale) had a binding affinity of −988.5 kcal/mol towards the SARS-CoV-2 spike glycoprotein which is comparable to the hACE2 binding affinity (−946.4 kcal/mol) to the spike glycoprotein. Thus, ACE2 and ACE2-like structures from the marine biota could be used as decoys for viral binding [ 197 ]. Fayed et al [ 198 ] screened several marine compounds for their pharmacophore potentials against SARS-CoV-2 Mpro (6lu7 and 6y2f), spike glycoprotein, and RNA Polymerase, and reported that compounds with a flavonoid core, acyl indole, and pyrrole carboxamide alkaloids performed better.…”

“…Heptafuhalol A (190), a phlorotannin fuhalol from Sargassum spinuligerum also exhibited strong binding affinity towards Mpro (−14.60 kcal/mol) by interacting with some amino acid residues within the protease receptor including Thr24, Ser46, Asn142, Glu166, and Pro168. Furthermore, other fuhalol and phlorthol phlorotannin including phlorethopentafuhalol A (191) and B (192), pseudopentafuhalol C (193), hydroxypentafuhalol A (194), pentaphlorethol B (195), aeruginosin 98B (196), resinoside B (197), pentaphlorethol A (198), and tunichrome An2 (199) also have promising SARS-CoV-2 protease inhibitory potentials. Also, the flavonoids -apigenin-7-O-neohesperidoside (rhoifolin) (200), luteolin-7-rutinoside (201), and resinoside B (197) (from the brown alga Sargassum spinuligerum) bind to SARS-CoV-2 Mpro with great affinity (−12.4 kcal/mol) [134].…”

“…Furthermore, other fuhalol and phlorthol phlorotannin including phlorethopentafuhalol A (191) and B (192), pseudopentafuhalol C (193), hydroxypentafuhalol A (194), pentaphlorethol B (195), aeruginosin 98B (196), resinoside B (197), pentaphlorethol A (198), and tunichrome An2 (199) also have promising SARS-CoV-2 protease inhibitory potentials. Also, the flavonoids -apigenin-7-O-neohesperidoside (rhoifolin) (200), luteolin-7-rutinoside (201), and resinoside B (197) (from the brown alga Sargassum spinuligerum) bind to SARS-CoV-2 Mpro with great affinity (−12.4 kcal/mol) [134]. Others have reported that apigenin (202) can interact with Mpro via H-bonds between the aromatic region and residues Leu141, Glu166, and Thr190, as well as π-stacking interaction with Gln189 [134].…”