| Autor: |
Wang, Yan, Zhang, Zhifang, Zhang, Ya, Yu, Cong |
| Zdroj: |
Luminescence: Journal of Biological & Chemical Luminescence; Jun2018, Vol. 33 Issue 4, p790-796, 7p |
| Abstrakt: |
Abstract: We have established a real‐time and label‐free fluorescence turn‐on strategy for protease activity detection and inhibitor screening via peptide‐induced aggregation‐caused quenching of a perylene probe. Because of electrostatic interactions and high hydrophilicity, poly‐ l‐glutamic acid sodium salt (PGA; a negatively charged peptide) could induce aggregation of a positively charged perylene probe (probe 1) and the monomer fluorescence of probe 1 was effectively quenched. After a protease was added, PGA was enzymatically hydrolyzed into small fragments and probe 1 disaggregated. The fluorescence recovery of probe 1 was found to be proportional to the concentration of protease in the range from 0 to 1 mU/ml. The detection limit was down to 0.1 mU/ml. In the presence of a protease inhibitor, protease activity was inhibited and fluorescence recovery reduced. Moreover, we demonstrated the potential application of our method in a complex mixture sample including 1% human serum. Our method is simple, fast and cost effective. [ABSTRACT FROM AUTHOR] |
| Databáze: |
Complementary Index |
| Externí odkaz: |
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