Natural compounds inhibit Monkeypox virus methyltransferase VP39 in silico studies

Quynh Mai Thai, Huong T.T. Phung, Ngoc Quynh Anh Pham, Jim Tong Horng, Phuong Thao Tran, Nguyen Thanh Tung, Son Tung Ngo*

*Corresponding author for this work

Research output: Contribution to journalJournal Article peer-review

1 Scopus citations


VP39, an essential 2′-O-RNA methyltransferase enzyme discovered in Monkeypox virus (MPXV), plays a vital role in viral RNA replication and transcription. Inhibition of the enzyme may prevent viral replication. In this context, using a combination of molecular docking and molecular dynamics (MDs) simulations, the inhibitory ability of NCI Diversity Set VII natural compounds to VP39 protein was investigated. It should be noted that the computed binding free energy of ligand via molecular docking and linear interaction energy (LIE) approaches are in good agreement with the corresponding experiments with coefficients of (Formula presented.) and 0.75, respectively. NSC 319990, NSC 196515 and NSC 376254 compounds were demonstrated that can inhibit MPVX methyltransferase VP39 protein with the similar affinity compared to available inhibitor sinefungin. Moreover, nine residues involving Gln39, Gly68, Gly72, Asp95, Arg97, Val116, Asp138, Arg140 and Asn156 may be argued that they play an important role in binding process of inhibitors to VP39. Communicated by Ramaswamy H. Sarma.

Original languageEnglish
JournalJournal of Biomolecular Structure and Dynamics
StateAccepted/In press - 2024

Bibliographical note

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© 2024 Informa UK Limited, trading as Taylor & Francis Group.


  • docking
  • LIE
  • MPVX
  • NCI
  • VP39


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