Tunable reactivation of nanoparticle-inhibited beta-galactosidase by glutathione at intracellular concentrations.
Tunable reactivation of nanoparticle-inhibited beta-galactosidase by glutathione at intracellular concentrations.
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DOI：
10.1021/ja046572r
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发表时间：
2004-10
影响因子：
15
通讯作者：
A. Verma;J. M. Simard;J. Worrall;V. Rotello
中科院分区：
文献类型：
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作者：
A. Verma;J. M. Simard;J. Worrall;V. Rotello
不同链长（C（8）和C（11））的带正电荷的三甲基铵官能化的混合单层保护簇（MMPC）已被用于通过互补静电相互作用结合β-半乳糖苷酶，导致完全的酶抑制。这种抑制作用可以在体外通过细胞内谷胱甘肽（GSH）（细胞的主要巯基成分）浓度来逆转。活性的恢复取决于单分子层的链长。细胞内浓度（1-10 mM）的GSH可完全恢复与C（8）单层颗粒结合的酶活性;然而，在细胞外GSH浓度下观察到很少或没有释放。相反，在任何研究浓度下，都没有观察到与C（11）颗粒结合的酶的恢复。总之，这些研究表明，GSH介导的酶结合MMPC的释放可以通过调节单层的结构，蛋白质和药物递送应用的重要工具。
Positively charged trimethylammonium-functionalized mixed monolayer protected clusters (MMPCs) of different chain lengths (C(8) and C(11)) have been used to bind beta-galactosidase through complementary electrostatic interactions, resulting in complete enzyme inhibition. This inhibition can be reversed in vitro by intracellular concentrations of glutathione (GSH), the main thiol component of the cell. The restoration of activity depends on the chain length of the monolayer. The activity of enzyme bound to particles with C(8) monolayer was completely restored by intracellular concentrations (1-10 mM) of GSH; however, little or no release was observed at extracellular GSH concentrations. In contrast, no restoration was observed for enzyme bound to the C(11) particles at any of the concentrations studied. Taken together, these studies demonstrate that the GSH-mediated release of enzymes bound to MMPCs can be tuned through the structure of the monolayer, a significant tool for protein and drug delivery applications.