期刊
FLUID PHASE EQUILIBRIA
卷 362, 期 -, 页码 349-354出版社
ELSEVIER SCIENCE BV
DOI: 10.1016/j.fluid.2013.10.052
关键词
Molecular dynamics; Myoglobin; Titanium dioxide; Protein adsorption; Molecular simulation
资金
- National Key Basic Research Program of China [2013CB733500]
- Program for New Century Excellent Talents in University [NCET-07-0313]
- National Natural Science Foundation of China [20706019, 20876052, 21376089]
- Guangdong Science Foundation [S2011010002078]
- State Key Laboratory of Materials-Oriented Chemical Engineering [KL12-05]
- Fundamental Research Funds for the Central Universities [SCUT-2013ZM0073]
The adsorption of myoglobin (Mb) on the surface of titanium dioxide is very important for the preparation of biosensors. Adsorption orientation and conformation of Mb on rutile (1 1 0) and (0 0 1) surfaces were investigated by combining Monte Carlo and molecular dynamics methods. The orientation, DSSP, super-imposed structure, root-mean-square deviation and gyration radius of Mb were analyzed. Furthermore, the distribution of water molecules on rutile (1 1 0) and (0 0 1) surfaces and representative snapshots of water molecules at different rutile interfaces were also discussed in detail. Simulation results show that adsorbed Mb conformations are not influenced by surfaces obviously because of the strong hydrophilicity of both surfaces. Two layers of water molecules form on both rutile (1 1 0) and (0 0 1) surfaces. After 80 ns molecular dynamics simulation, the heme of Mb is close to the rutile (0 0 1) surface and far away from the rutile (1 1 0) surface; this infers that electron transfer pathway of Mb is closer to the rutile (0 0 1) surface, which is favorable for faster electron transfer. (C) 2013 Elsevier B.V. All rights reserved.
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