Hydrophobic and Hofmeister effects on the adhesion of spider silk proteins onto solid substrates: An AFM-based single-molecule study
Hydrophobic and Hofmeister effects on the adhesion of spider silk proteins onto solid substrates: An AFM-based single-molecule study
复制标题
DOI：
10.1021/la702341j
复制
发表时间：
2008-02-19
期刊：
影响因子：
3.9
通讯作者：
Hugel, Thorsten
中科院分区：
文献类型：
--
作者：
Geisler, Michael;Pirzer, Tobias;Hugel, Thorsten
基于原子力显微镜的单分子力谱研究了Hofmeister盐和蛋白质疏水性对重组蜘蛛丝蛋白在固体基质上粘附的影响。因此，一种由蜘蛛丝蛋白和AFM针尖组成的分子探针已经被开发出来，它(i)是一个定义良好的小系统，可以通过分子动力学模拟来模拟，（ii）允许访问离子的整个可溶浓度范围，（iii）提供解吸力的分布，而不仅仅是集合平均平均值。测定的阴离子（H2PO4-, Cl-, I-）的解吸力符合Hofmeister级数，对5 M NaH2PO4稳定能大于15 k(B)T。此外，这种效应还受到蛛丝蛋白疏水性的影响，说明疏水性与霍夫迈斯特效应密切相关。
AFM-based single-molecule force spectroscopy has been used to study the effect of Hofmeister salts and protein hydrophobicity on the adhesion of recombinant spider silk proteins onto solid substrates. Therefore, a molecular probe consisting of a spider silk protein and an AFM tip has been developed, which (i) is a well-defined, small system that can be simulated by molecular dynamics simulations, (ii) allows access to the whole soluble concentration range for ions, and (iii) provides the distribution of desorption forces rather than just ensemble-averaged mean values. The measured desorption forces follow the Hofmeister series for anions (H2PO4-, Cl-, I-) with a stabilizing energy of more than 15 k(B)T for 5 M NaH2PO4. Moreover, this effect is influenced by the hydrophobicity of the spider silk protein, indicating that hydrophobic and Hofmeister effects are closely related.