Marine fungal diversity unlocks potent antivirals against monkeypox through methyltransferase inhibition revealed by molecular dynamics and free energy landscape

Table 2 Intermolecular interaction for the selected compound docked against methyltransferase VP39

S. no	Protein–ligand complex	Hydrogen bond	Hydrophobic interaction	π–π stacking/ π–π cation* interaction	Salt Bridge Interaction	Halogen bond interaction
1	Methyltransferase VP39- CMNPD15724	Asp¹³⁸,Ser¹⁴¹, Val¹¹⁶, Arg⁹⁷ Arg¹⁴⁰ Asp⁹⁵	Leu⁴², Val¹³⁹, Ala⁷⁰, Ile⁶⁷, Leu¹⁵⁹, Val¹¹⁶, Ile⁹⁴, Phe¹¹⁵	–		Ile⁹⁴ and Val¹¹⁶
2	Methyltransferase VP39-CMNPD28811	Asp¹³⁸	Leu¹⁵⁹, Val¹¹⁶, Phe¹¹⁵, Ile⁹⁴, Val¹³⁹, Ile⁶⁷, Ala⁷⁰	Phe¹¹⁵
3	Methyltransferase VP39-CMNPD30883	Gly⁷² Gln³⁹	Val¹¹⁶, Phe¹¹⁵, Leu¹⁵⁹, Tyr⁶⁶, Ile⁶⁷, Ala⁷⁰, Pro⁷¹, Leu⁴², Ile⁷⁵, Val¹³⁹	–	Arg⁹⁷
4	Methyltransferase VP39-CMNPD18569	Gly⁶⁸, Asp¹³⁸, Arg¹⁴⁰, Asp⁹⁵, Arg⁹⁷, and Val¹¹⁶	Leu¹⁵⁹, Val¹¹⁶, Phe¹¹⁵, Val¹³⁹, Ala⁷⁰, Ile⁶⁷ and Ile⁹⁴	Phe¹¹⁵
5	Methyltransferase VP39-sinefungin (control)	Asp⁹⁵, Arg¹⁴⁰, Asp¹³⁸, Try⁶⁶, Gln³⁹, Gly⁷² Val¹¹⁶	Ile⁹⁴, Phe¹¹⁵,Val¹¹⁶, Leu¹⁵⁹, Ile⁷⁵, Leu⁴², Pro⁷¹, Ala⁷⁰, Ile⁶⁷, Tyr⁶⁶ and Val¹³⁹	Phe¹¹⁵

*π–π stacking/π–π cation interaction: This indicates the interactions between aromatic rings (π–π stacking) or between an aromatic ring and a cation (π–π cation)

ISSN: 2661-801X