Amphiphilic amino acids: a key to adsorbing proteins to nanopatterned surfaces?
Amphiphilic amino acids: a key to adsorbing proteins to nanopatterned surfaces?
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DOI：
10.1039/c2sc21639f
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发表时间：
2013-01-01
期刊：
影响因子：
8.4
通讯作者：
Yarovsky, Irene
中科院分区：
文献类型：
--
作者：
Hung, Andrew;Mager, Morgan;Yarovsky, Irene
已经表明，两亲性氨基酸在蛋白质在具有有序的条纹域结构的纳米结构表面上的吸附中起重要作用，例如由单层保护的金属纳米颗粒（MPMN）呈现的那些。我们已经提出，现在进一步探讨这一假设，通过研究蛋白质的吸附行为MPMN表面的分子动力学（MD）模拟。我们的原子分子动力学模拟溶菌酶（Lyz）的纳米结构的表面，包括单组分表面和几个理论的纳米粒子的不同间距，这里提出的证实了特殊的作用，含有侧链胺的氨基酸促进蛋白质直接吸附到MPMN表面。虽然我们之前已经证明了两亲性氨基酸赖氨酸负责Cyt C在纳米结构表面上的选择性吸附行为，但在Lyz的情况下，精氨酸的两亲性特征使蛋白质能够同时与极性和非极性表面配体形成紧密接触。这使得它对于与由相邻纳米级化学域组成的表面的相互作用特别重要。Arg还能够与均相的疏水和亲水配体表面形成紧密接触。我们还发现，其他两亲性氨基酸，如酪氨酸和色氨酸，通过水介导的接触与表面相互作用。桥接水分子采用不同于简单表面吸附沃茨的取向，其取向的特异性促进蛋白质-表面接触。我们的研究结果表明，不仅纳米图案化的表面可以被设计为选择性地与不同的蛋白质相互作用，而且蛋白质可以被设计为通过有针对性地掺入合成氨基酸来与纳米材料特异性地相互作用，所述合成氨基酸可以模拟对不同化学基序具有多种亲和力的天然两亲性氨基酸。
It has been suggested that amphiphilic amino acids play an important role in the adsorption of proteins on nanostructured surfaces with an ordered, striped domain structure such as those presented by monolayer-protected metal nanoparticles (MPMNs). We have proposed and now further explore this hypothesis by studying the adsorption behaviour of proteins on MPMN surfaces by molecular dynamics (MD) simulations. Our atomistic MD simulations of lysozyme (Lyz) on nanostructured surfaces, including single component surfaces and several theoretical nanopatterns of different spacing, presented here confirm the special role of amino acids containing sidechain amines in facilitating direct protein adsorption to MPMN surfaces. While we have previously demonstrated that an amphiphilic amino acid lysine is responsible for selective adsorption behaviour of Cyt C on nanostructured surfaces, in the case of Lyz it is the amphipathic character of arginine that enables the protein to form close contacts with both polar and non-polar surface ligands simultaneously. This renders it especially important for interactions with surfaces composed of adjacent nano-scale chemical domains. Arg is also capable of forming close contacts with homogeneous hydrophobic and hydrophilic ligand surfaces. We have also found that other amphiphilic amino acids, such as tyrosine and tryptophan, interact with surfaces via water-mediated contacts. Bridging water molecules adopt orientations which differ from those of simple surface-adsorbed waters, with the specificity of their orientations facilitating the protein-surface contacts. Our findings suggest that not only nanopatterned surfaces can be designed to selectively interact with different proteins but proteins may be engineered to specifically interact with nanomaterials by targeted incorporation of synthetic amino acids which can mimic natural amphiphilic amino acids possessing multiple affinities to different chemical motifs.