C60@Lysozyme: Direct Observation by Nuclear Magnetic Resonance of a 1:1 Fullerene Protein Adduct
C60@Lysozyme: Direct Observation by Nuclear Magnetic Resonance of a 1:1 Fullerene Protein Adduct
复制标题
DOI：
10.1021/nn4063374
复制
发表时间：
2014-02-01
期刊：
影响因子：
17.1
通讯作者：
Zerbetto, Francesco
中科院分区：
文献类型：
--
作者：
Calvaresi, Matteo;Arnesano, Fabio;Zerbetto, Francesco
将碳纳米颗粒（CNPs）与蛋白质结合形成混合功能组装体是一个创新的研究领域，在医学、纳米技术和材料科学方面具有很大的前景。对CNP-蛋白质相互作用的理解需要对CNP的“结合口袋”的识别和表征。在这里，使用溶菌酶和C-60作为模型系统和NMR化学位移扰动分析，蛋白质-CNP结合口袋在溶液中被明确识别，并且在单个氨基酸水平上的结合效果的特征在于各种实验和计算方法。溶菌酶与C-60形成化学计量1：1加合物，其单分子分散在水中。溶菌酶在与C-60相互作用后保持其三维结构，并且只有少数鉴定的残基被扰动。C-60识别是高度特异性的，并且定位在一个明确的口袋中。
Integrating carbon nanoparticles (CNPs) with proteins to form hybrid functional assemblies is an innovative research area with great promise for medical, nanotechnology, and materials science. The comprehension of CNP-protein interactions requires the still-missing identification and characterization of the 'binding pocket' for the CNPs. Here, using Lysozyme and C-60 as model systems and NMR chemical shift perturbation analysis, a protein-CNP binding pocket is identified unambiguously in solution and the effect of the binding, at the level of the single amino acid, is characterized by a variety of experimental and computational approaches. Lysozyme forms a stoichiometric 1:1 adduct with C-60 that is dispersed monomolecularly in water. Lysozyme maintains its tridimensional structure upon interaction with C-60 and only a few identified residues are perturbed. The C-60 recognition is highly specific and localized in a well-defined pocket.