PHYTOCHEMICAL TO INTERACT WITH NLS BINDING SITE ON IMA3 TO INHIBIT IMPORTIN Α/Β1 MEDIATED NUCLEAR IMPORT OF SARS-COV-2 CARGO

  • BHARATH B. R. Atrimed Biotech LLP, BBC, Electronics City Phase 1, Electronic City, Bengaluru, Karnataka 560100
  • HRISHIKESH DAMLE Atrimed Pharmaceuticals Pvt. Ltd. 14th Floor no 29, Prestige Meridian Tower 2, 30, Mahatma Gandhi Rd, KG Halli, D' Souza Layout, Ashok Nagar, Bengaluru, Karnataka 560001
  • SHIBAN GANJU Atrimed Pharmaceuticals Pvt. Ltd. 14th Floor no 29, Prestige Meridian Tower 2, 30, Mahatma Gandhi Rd, KG Halli, D' Souza Layout, Ashok Nagar, Bengaluru, Karnataka 560001
  • LATHA DAMLE Atrimed Biotech LLP, BBC, Electronics City Phase 1, Electronic City, Bengaluru, Karnataka 560100

Abstract

Objective: Ivermectin is an FDA-approved, broad-spectrum anti-parasitic agent. It was originally identified as an inhibitor of interaction between the human 29 immunodeficiency virus-1 (HIV-1) integrase protein (IN) and the Importin (IMP) α/β1 30 heterodimers, which are responsible for IN nuclear import. Recent studies demonstrate that ivermectin is worthy of further consideration as a possible SARS-CoV-2 antiviral.


Methods: We built the pathogen-host interactome and analyzed it using PHISTO. We compared Ivermectin and plant molecules for their interaction with Importin α3 (IMA3) using molecular docking studies.


Results: A phytochemical ATRI001 with the lowest binding energy-7.290 Kcal/mol was found to be superior to Ivermectin with binding energy-4.946 Kcal/mol.


Conclusion: ATRI001 may be a potential anti-SARS-CoV-2 agent; however, it requires clinical evaluation.

Keywords: Ivermectin, SARS-CoV-2, IMA3, Phytochemical and Molecular docking

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B. R., B., H. DAMLE, S. GANJU, and L. DAMLE. “PHYTOCHEMICAL TO INTERACT WITH NLS BINDING SITE ON IMA3 TO INHIBIT IMPORTIN Α/Β1 MEDIATED NUCLEAR IMPORT OF SARS-COV-2 CARGO”. International Journal of Pharmacy and Pharmaceutical Sciences, Vol. 12, no. 8, June 2020, pp. 30-35, doi:10.22159/ijpps.2020v12i8.38184.
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