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| Content Provider | Springer Nature Link |
|---|---|
| Author | Nguyen, Hung Le, Ly |
| Copyright Year | 2015 |
| Abstract | We have used steered molecular dynamics simulation to investigate the molecular interactions between four M2 inhibitors (amantadine, rimantadine, and two other amantadine derivatives) and the M2 protein channels of influenza A virus H5N1, including the wild type (WT) and three previously identified drug-resistant variants (G34A, S31N, and V27A). The binding free energies between these four inhibitors and the M2 channel of the WT and the three mutants were also determined by use of the molecular mechanics–Poisson–Boltzmann surface area method. Our study provides important insight into binding affinity, including detailed energy components and interactions at the molecular level of four potential inhibitors with the M2 channel of drug-resistant strains; this may assist further experimental study and strategies for rational design of new inhibitors. |
| Starting Page | 447 |
| Ending Page | 455 |
| Page Count | 9 |
| File Format | |
| ISSN | 01757571 |
| Journal | European Biophysics Journal |
| Volume Number | 44 |
| Issue Number | 6 |
| e-ISSN | 14321017 |
| Language | English |
| Publisher | Springer Berlin Heidelberg |
| Publisher Date | 2015-06-02 |
| Publisher Place | Berlin, Heidelberg |
| Access Restriction | One Nation One Subscription (ONOS) |
| Subject Keyword | Influenza A virus M2 channel proteins Drugs A1 (amantadine), A2 (rimantadine), A3, and A4 Wild type, G34A, S31N, and V27A mutants Binding energy Drug design Biochemistry Biophysics and Biological Physics Cell Biology Neurobiology Membrane Biology Nanotechnology |
| Content Type | Text |
| Resource Type | Article |
| Subject | Medicine Biophysics |
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