Humboldt-Universität zu Berlin, Department of Chemistry, Brook-Taylor-Str. 2, 12489 Berlin, Germany.
Analyst. 2018 Dec 3;143(24):6061-6068. doi: 10.1039/c8an01321g.
The interaction of bovine serum albumin (BSA) and human serum albumin (HSA), sharing a sequence similarity of 77.5%, with gold nanoparticles of a size of ∼30 nm was investigated by surface-enhanced Raman scattering (SERS). The spectra provide information on those residues of the proteins in proximity of the nanoparticles. The SERS signals indicate an electrostatic interaction of both proteins with the citrate ligands at the nanoparticle surface via lysine residues. HSA, different from BSA also binds directly to the gold surface by particularly flexible protein segments that were identified by comparison of the vibrational bands with the known amino acid sequence of the molecule. The data suggest that both the direct binding as well as interaction with the citrate ligands determine the interaction, yet to varying extent in the two very similar serum proteins. This has implications for their use in bio-functionalization, and for the application of gold nanostructures in bioanalytics and medicine.
通过表面增强拉曼散射（SERS）研究了大小约为 30nm 的金纳米粒子与具有 77.5%序列相似性的牛血清白蛋白（BSA）和人血清白蛋白（HSA）之间的相互作用。该光谱提供了有关那些靠近纳米粒子的蛋白质残基的信息。SERS 信号表明，两种蛋白质都通过赖氨酸残基通过静电相互作用与纳米粒子表面的柠檬酸盐配体相互作用。与 BSA 不同的是，HSA 还通过特别灵活的蛋白质片段直接与金表面结合，这些片段通过与已知分子的氨基酸序列进行比较而被识别。数据表明，直接结合以及与柠檬酸盐配体的相互作用都决定了相互作用，但在两种非常相似的血清蛋白中程度不同。这对它们在生物功能化中的应用以及对金纳米结构在生物分析和医学中的应用都有影响。
