Fe(III)-mediated reversible catalytic activity of MoS nanozymes for bisphosphonate drug sensing.

Peroxidase-like activity of MoS quantum dots (QDs) can be reversibly regulated by means of Fe/alendronate sodium (ALDS)-induced aggregation/disaggregation of the QDs in solution. Specifically, Fe can selectively aggregate the MoS QDs and thus greatly enhance their peroxidase-like activity, while such enhancement can be inhibited in the presence of ALDS owing to the competitive coordination of ALDS with Fe. By regulating the enzyme-like activity of MoS QDs, different colorimetric signal of a typical substrate of horseradish peroxidase, 3,3΄,5,5΄-tetramethylbenzidine, can be measured in the presence of HO.

Aggregation/dispersion-mediated peroxidase-like activity of MoS quantum dots for colorimetric pyrophosphate detection.

Peroxidase-like activity of MoS2 quantum dots can be manipulated by aggregation/dispersion in the presence of Fe3+ or a mix of Fe3+ and pyrophosphate (PPi). Based on this finding, a simple and reliable method for colorimetric PPi detection is developed.

ΔNp63α modulates phosphorylation of p38 MAP kinase in regulation of cell cycle progression and cell growth.

p53-related p63 plays a critical role in regulation of cell proliferation, survival and cell differentiation. Dysregulation of p63 functions results in a disruption of a variety of normal biological processes, including stem cell biology, embryonic development, aging and tumorigenesis. ΔNp63α, a predominantly expressed p63 protein isoform in epithelial cells, plays a crucial role in regulation of cell cycle progression and cell growth.