(School of Chemical Engineering and Technology, Tianjin University, Tianjin 300072, China; Key Laboratory of Systems Bioengineering, Ministry of Education, Tianjin University, Tianjin 300072, China)
Abstract Virus-like particles (VLP) is a selfassembly of capsomere (Cap) with great potential in vaccinology, gene therapy, drug delivery, and materials science. The stability of Cap is crucial for its selfassembly to VLP. In the present study, the allatom molecular dynamics (MD) simulations are performed to investigate the effect of solution conditions on the stabilization of Cap. The conformational transition has been investigated. The structure of solvent is also examined to explore the molecular mechanism of the regulation on the stabilization of Cap by solution conditions. In both stabilization buffer and aqueous solution, Na+ can be attracted and accumulated around protein through electrostatic interaction, and forms a shell with water molecules. This is very important for the stabilization of Cap. Moreover, in stabilization buffer, the shell formed by accumulated Na+ around the protein can induce the formation of a shell of Cl-. The multishell structure causes more hydrogen bonds within Cap and consequently provides better stabilization of Cap. These results provide molecular insights into the effect of solution condition on the stabilization of Cap, which would be beneficial for the regulation of VLP selfassembly.
2013, Vol. 30 
