Xie Mouzhe, Hansen Alexandar L, Yuan Jiaqi, Brüschweiler Rafael
Department of Chemistry and Biochemistry, The Ohio State University, Columbus, Ohio 43210, United States.
Campus Chemical Instrument Center, The Ohio State University, Columbus, Ohio 43210, United States.
J Phys Chem C Nanomater Interfaces. 2016 Oct 27;120(42):24463-24468. doi: 10.1021/acs.jpcc.6b08213. Epub 2016 Sep 21.
Elucidation of the driving forces that govern interactions between nanoparticles and intrinsically disordered proteins (IDP) is important for the understanding of the effect of nanoparticles in living systems and for the design of new nanoparticle-based assays to monitor health and combat disease. The quantitative interaction profile of the intrinsically disordered transactivation domain of p53 and its mutants with anionic silica nanoparticles is reported at atomic resolution using nuclear magnetic spin relaxation experiments. These profiles are analyzed with a novel interaction model that is based on a quantitative nanoparticle affinity scale separately derived for the 20 natural amino acids. The results demonstrate how the interplay of attractive and repulsive Coulomb interactions with hydrophobic effects is responsible for the sequence-dependent binding of a disordered protein to nanoparticles.
阐明支配纳米颗粒与内在无序蛋白质（IDP）之间相互作用的驱动力，对于理解纳米颗粒在生物系统中的作用以及设计基于纳米颗粒的新型检测方法以监测健康状况和对抗疾病至关重要。利用核磁共振自旋弛豫实验，在原子分辨率下报道了p53及其突变体的内在无序反式激活结构域与阴离子二氧化硅纳米颗粒的定量相互作用谱。这些谱通过一种新型相互作用模型进行分析，该模型基于分别为20种天然氨基酸推导的定量纳米颗粒亲和力标度。结果表明，吸引和排斥库仑相互作用与疏水效应之间的相互作用如何导致无序蛋白质与纳米颗粒的序列依赖性结合。
