Skepö M
Health and Society, Malmö University, S-205 06 Malmö, Sweden.
J Chem Phys. 2008 Nov 14;129(18):185101. doi: 10.1063/1.3002317.
The structural properties of the salivary protein statherin upon adsorption have been examined using a coarse-grained model and Monte Carlo simulation. A simple model system with focus on electrostatic interactions and short-ranged attractions among the uncharged amino acids has been used. To mimic hydrophobically modified surfaces, an extra short-ranged interaction was implemented between the amino acids and the surface. It has been shown that the adsorption and the thickness of the adsorbed layer are determined by (i) the affinity for the surface, i.e., denser layer with an extrashort-ranged potential, and (ii) the distribution of the charges along the chain. If all the amino acids have a high affinity for the surface, the protein adsorbs in a train conformation, if the surface is negatively charged the protein adsorbs in a tail-train conformation, whereas if the surface is positively charged the protein adsorbs in a loop conformation. The latter gives rise to a more confined adsorbed layer.
利用粗粒度模型和蒙特卡罗模拟研究了唾液蛋白（组蛋白）吸附后的结构特性。采用了一个简单的模型系统，重点关注静电相互作用以及不带电氨基酸之间的短程吸引力。为了模拟疏水改性表面，在氨基酸与表面之间引入了额外的短程相互作用。结果表明，吸附层的吸附和厚度取决于：（i）对表面的亲和力，即具有超短程势的较致密层；（ii）电荷沿链的分布。如果所有氨基酸对表面都有高亲和力，蛋白质以伸展链构象吸附；如果表面带负电，蛋白质以尾-伸展链构象吸附；而如果表面带正电，蛋白质以环构象吸附。后者会导致吸附层更受限。
