Search Swinburne Research Bank
This object has not yet been indexed by the background indexing service.
Please use this identifier to cite or link to this item: http://hdl.handle.net/1959.3/58000
|Download PDF (Published version) (Adobe Acrobat PDF, -1 bytes)|
- Coarse-grained molecular dynamics of ligands binding into protein: the case of HIV-1 protease inhibitors
- Li, Dechang; Liu, Ming S.; Ji, Baohua; Hwang, Kehchih; Huang, Yong Gang
- Binding dynamics and pathways of ligands or inhibitors to target proteins are challenging both experimental and theoretical biologists. A dynamics understanding of inhibitors interacting with protein is essential for the design of novel potent drugs. In this work we applied a coarse-grained molecular dynamics method for simulating inhibitors entering the binding cavity of human immunodeficiency virus type 1 protease (PR). It shows that the coarse-grained dynamics, consistent with the experimental results, can capture the essential molecular dynamics of various inhibitors binding into PR. The primary driving force for the binding processes is the nonbond interaction between inhibitors and PR. The size and topology of inhibitors and the interacting strength between inhibitors and PR have great influence on the binding mode and processes. The interaction strength between the PR and various inhibitors is also analyzed by atomistic molecular mechanics and Poisson-Boltzmann solvation area method.
- Publication type
- Journal article
- Research centre
- Swinburne University of Technology. Faculty of Information and Communication Technologies. Centre for Molecular Simulation
- Journal of Chemical Physics, Vol. 130, no. 21 (Jun 2009), p. 10
- Publication year
- American Institute of Physics
- Publisher URL
- Copyright © 2009 American Institute of Physics. Published version of this paper reproduced here in accordance with the copyright policy of the publisher.