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Novel binding patterns between ganoderic acids and neuraminidase: Insights from docking, molecular dynamics and
Zhiwei Yang1, Fei Wu2, Xiaohui Yuan3
1Department of Applied Physics, Xi'an Jiaotong University, Xi'an 710049, PR China; School of Basic Medical Sciences, Jiamusi University, Jiamusi 154007, PR China.
Journal of Molecular Graphics & Modelling
|February 25, 2016
Summary
Ganoderic acids show promise as novel neuraminidase (NA) inhibitors, with ganoderic acid DM exhibiting strong binding affinity and a unique interaction pattern against influenza virus mutations.
Area of Science:
- Biochemistry
- Computational Chemistry
- Pharmacology
Background:
- Ganoderic acids (GAs) are emerging as potential neuraminidase (NA) inhibitors.
- Understanding the binding patterns of GAs with NA is crucial for drug development.
Purpose of the Study:
- To investigate the binding profiles of GAs with the N1 neuraminidase protein, including H274Y and N294S mutations.
- To compare the binding affinities of GAs with oseltamivir.
- To elucidate the key interactions and driving forces in GA-NA binding.
Main Methods:
- Molecular docking
- Molecular dynamics simulations
- MM/PBSA calculations
Main Results:
- Ganoderic acid DM and Z showed binding affinities comparable to oseltamivir.
- Electrostatic interactions were identified as the primary driving force for binding.
- Ganoderic acid DM demonstrated a novel binding pattern, steric hindrance in the 150 cavity, and activity against resistant mutations.
Conclusions:
- Ganoderic acid DM is a promising anti-influenza candidate with advantages over oseltamivir.
- Key residues Asp151 and Arg152 in the 150-loop are important for binding.
- Findings provide insights for designing effective dual-site NA inhibitors.
