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<p>Nipah virus (NiV) is a highly pathogenic zoonotic virus associated with severe encephalitis and respiratory illness, with high mortality rates and no approved specific antiviral therapy. The nucleocapsid (N) protein plays a crucial role in viral genome encapsidation and replication, making it a promising therapeutic target. Identifying effective inhibitors against the NiV N protein is therefore of significant clinical importance. This study employed a structure-based virtual screening approach to identify potential inhibitors targeting the NiV N protein. A antiviral compound library was screened using molecular docking, drug-likeness, and ADME profiling. Two lead molecules 7-Deacetoxy-7-oxogedunin and 4-Methoxynorsecurinine were shortlisted based on estimated binding affinity and intermolecular non-covalent interactions. Triplicate molecular dynamics simulations assessed complex stability through RMSD, RMSF, Rg, and SASA analyses. Principal Component Analysis revealed ligand-induced conformational flexibility. MM/PBSA based binding free energy calculations demonstrated stronger binding for 7-Deacetoxy-7-oxogedunin (− 28.48&#xa0;kcal/mol) compared to 4-Methoxynorsecurinine (− 15.19&#xa0;kcal/mol). Among the screened compounds, 7-Deacetoxy-7-oxogedunin exhibited superior binding stability, emerging as the most promising inhibitor. These findings provide a robust computational framework and a rational basis for further experimental validation and antiviral drug development targeting the NiV N protein.</p>

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Structure-Based identification and triplicate molecular dynamics evaluation of phytochemical inhibitors targeting the nipah virus nucleocapsid protein

  • 期刊论文

  • 发表日期：

    2026年7月28日

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  • Ayesha Parvez,
  • Manisha Sangwan,
  • Roopali Bhati,
  • Pragati Mahur,
  • Abhishek Sharma,
  • Jayaraman Muthukumaran,
  • Amit Kumar Singh,
  • Monika Jain

摘要

Nipah virus (NiV) is a highly pathogenic zoonotic virus associated with severe encephalitis and respiratory illness, with high mortality rates and no approved specific antiviral therapy. The nucleocapsid (N) protein plays a crucial role in viral genome encapsidation and replication, making it a promising therapeutic target. Identifying effective inhibitors against the NiV N protein is therefore of significant clinical importance. This study employed a structure-based virtual screening approach to identify potential inhibitors targeting the NiV N protein. A antiviral compound library was screened using molecular docking, drug-likeness, and ADME profiling. Two lead molecules 7-Deacetoxy-7-oxogedunin and 4-Methoxynorsecurinine were shortlisted based on estimated binding affinity and intermolecular non-covalent interactions. Triplicate molecular dynamics simulations assessed complex stability through RMSD, RMSF, Rg, and SASA analyses. Principal Component Analysis revealed ligand-induced conformational flexibility. MM/PBSA based binding free energy calculations demonstrated stronger binding for 7-Deacetoxy-7-oxogedunin (− 28.48 kcal/mol) compared to 4-Methoxynorsecurinine (− 15.19 kcal/mol). Among the screened compounds, 7-Deacetoxy-7-oxogedunin exhibited superior binding stability, emerging as the most promising inhibitor. These findings provide a robust computational framework and a rational basis for further experimental validation and antiviral drug development targeting the NiV N protein.