Gold nanoparticle cytochrome c complexes: The effect of nanoparticle ligand charge on protein structure
Gold nanoparticle cytochrome c complexes: The effect of nanoparticle ligand charge on protein structure
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DOI：
10.1021/la052102e
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发表时间：
2005-12-20
期刊：
影响因子：
3.9
通讯作者：
Hamad-Schifferli, K
中科院分区：
文献类型：
--
作者：
Aubin-Tam, ME;Hamad-Schifferli, K
我们报告了纳米粒子配体电荷对共价、位点特异性连接的蛋白质结构的影响。将具有阳性、阴性和中性配体的纳米颗粒附加到酿酒酵母细胞色素c的特定半胱氨酸C102上。通过 HPLC 或凝胶电泳纯化缀合物。圆二色光谱表明，改变纳米粒子配体会显着影响附着的细胞色素 c 结构。该蛋白质在中性配体的情况下保留其结构，但在带电物质存在时会变性。这是通过 C102 局部附近的氨基酸与配体端基的静电相互作用来合理化的。
We report the effect of nanoparticle ligand charge on the structure of a covalently, site-specifically linked protein. An nanoparticles with positive, negative, and neutral ligands were appended to a specific cysteine, C102, of Saccharomyces cerevisiae cytochrome c. Conjugates were purified by HPLC or gel electrophoresis. Circular dichroism spectroscopy shows that changing the nanoparticle ligand dramatically influences the attached cytochrome c structure. The protein retains its structure with neutral ligands but denatures in the presence of charged species. This is rationalized by the electrostatic interaction of amino acids in the local vicinity of C102 with the endgroups of the ligand.