期刊
LANGMUIR
卷 27, 期 18, 页码 11591-11596出版社
AMER CHEMICAL SOC
DOI: 10.1021/la202405t
关键词
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资金
- National Science Foundation [0847957, 0618242]
- Robert A. Welch Foundation [F-0032]
- Division Of Chemistry
- Direct For Mathematical & Physical Scien [0847957] Funding Source: National Science Foundation
Here, we report that a conductive Au@Ag2O nanoparticle structure significantly enhances the stability of alkaline phosphatase (AlkP) in the presence of the inhibitors urea and L-phenylalanine (Phe). The enzyme/nanoparticle construct is prepared by associating the enzyme with citrate-capped Au particles, and then adding Ag+. UV-vis and XPS spectroscopy and transmission electron microscopy confirm the core@shell structure. AlkP activity was quantified in the presence and absence of the two inhibitors using a time-resolved colorimetric assay. The results indicate that 21% of the initial active AlkP is incorporated into the nanoparticle structure. More importantly, however, the Au@Ag2O core@shell host reduces the inhibitory effect of urea and Phe by factors ranging from 3 to 12, depending on the inhibitor and its concentration, compared to the wildtype enzyme.
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