Citation: HU Li-Mei, LIN Cun-Guo, WANG Li, YUAN Shi-Ling. Lysozyme Protein Adsorbed on Antifouling Polymer Film Surface[J]. Acta Physico-Chimica Sinica, ;2014, 30(11): 2149-2156. doi: 10.3866/PKU.WHXB201409021 shu

Lysozyme Protein Adsorbed on Antifouling Polymer Film Surface

HU Li-Mei ^1,2 ,
LIN Cun-Guo ² ,
WANG Li ² ,
YUAN Shi-Ling ^1,

1.
1. Key Laboratory of Colloid and Interface Chemistry, Shandong University, Jinan 250100, P. R. China;
2. State Key Laboratory for Marine Corrosion and Protection, Luoyang Ship Material Research Institute LSMRI, Qingdao 266101, Shandong Province, P. R. China

Received Date: 31 July 2014
Available Online: 2 September 2014
Fund Project: 国家重点基础研究发展规划项目(973) (2014CB643305)资助 (973) (2014CB643305)

Molecular dynamics simulations were used to compare the adsorption behavior of lysozyme on two typical antifouling polymer materials: poly(ethylene) glycol (PEG) and poly(dimethylsiloxane) (PDMS). The influence of the surface properties of the polymer films on protein adsorption is discussed at the microscale. Based on the interactions, energy changes between the protein and polymer films, and dynamical behavior of the hydration molecules near the polymer film, the reasons why the PEG antifouling coating has a better antifouling effect than the PDMS surface were determined as follows. (1) The lower binding energy between the protein and the PEG coating than between the protein and the PDMS coating makes the protein adsorb weaker on the PEG coating than on the PDMS coating. (2) The protein would adsorb on the film surface when overcoming the energy barrier caused by the hydration layer. Molecular water adsorbs on the PEG surface stronger than on the PDMS surface, and is difficult to desorb. Therefore, the protein needs to overcome a higher energy barrier to adsorb to the PEG surface than to the PDMS surface, and thus it is more difficult for protein to absorb on the PEG surface than on the PDMS surface.
- Poly(ethylene) glycol,
- Poly(dimethylsiloxane),
- Antifouling material,
- Molecular dynamics
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