Sun Tianyang, Han Guang, Lindgren Matteus, Shen Zhijian, Laaksonen Aatto
Soft Matter Research Center and Department of Chemistry, Zhejiang University, 310027 Hangzhou, P. R. China.
Biomater Sci. 2014 Aug 30;2(8):1090-1099. doi: 10.1039/c4bm00021h. Epub 2014 May 1.
Binding of the proteins human lactoferrin (LF) and human bone morphogenetic protein-2 (BMP2) to a hydroxylated TiO rutile (110) surface has been modeled using molecular dynamics (MD) simulations. In order to study the effect of the hydrophobicity of the rutile surface on the protein binding process, the rutile surface was made more hydrophilic or more hydrophobic by adjusting the rutile atomic charges. The binding of LF and BMP2 to the hydrophobic rutile surface occurred through direct contact between the protein and rutile via both hydrophobic and hydrophilic amino acids. This forced the proteins to undergo structural rearrangements, observed primarily in BMP2. Binding to the hydrophilic rutile surface was largely indirect via the hydration layer of water on the surface of rutile. Both LF and BMP2 had a higher binding strength to the hydrophobic rutile surfaces than to the hydrophilic surfaces, as seen in the larger amplitude of the binding energies.
利用分子动力学（MD）模拟对人乳铁蛋白（LF）和人骨形态发生蛋白-2（BMP2）与羟基化二氧化钛金红石（110）表面的结合进行了建模。为了研究金红石表面疏水性对蛋白质结合过程的影响，通过调整金红石原子电荷使金红石表面更亲水或更疏水。LF和BMP2与疏水金红石表面的结合是通过蛋白质与金红石之间通过疏水和亲水氨基酸的直接接触发生的。这迫使蛋白质发生结构重排，主要在BMP2中观察到。与亲水金红石表面的结合主要是通过金红石表面的水合层间接发生的。如结合能的较大振幅所示，LF和BMP2与疏水金红石表面的结合强度均高于与亲水表面的结合强度。
