Journal
ANALYTICAL CHEMISTRY
Volume 88, Issue 6, Pages 3363-3368Publisher
AMER CHEMICAL SOC
DOI: 10.1021/acs.analchem.6b00036
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Funding
- Collaborative Innovation Center of Suzhou Nano Science and Technology
- Hefei Science Center CAS [2015HSC-UP012]
- National Natural Science Foundation of China [U1332142, 21375121]
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Tyrosine kinase and phosphatase are two important, antagonistic enzymes in organisms. Development of noninvasive approach for sensing their activity with high spatial and temporal resolution remains challenging. Herein, we rationally designed a hydrogelator Nap-Phe-Phe(CF3)-Glu-Tyr-Ile-OH (1a) whose supramolecular hydrogel (i.e., Gel 1a) can be subjected to tyrosine kinase-directed disassembly, and its phosphate precursor Nap-Phe-Phe(CF3)-Glu-Tyr(H2PO3)-Ile-OH (1b) which: can be subjected to alkaline phosphatase (ALP)-instructed self-assembly to fonn supramolecular hydro gel Gel 1b, respectively.. Mechanic properties and internal fibrous networks of the hydrogels were characterized with rheology and cryo transmission electron microscopy (cryo-TEM). Disassembly/Self-asSemblY of their corresponding supramolecular hydrogels conferring respective On/Off' F-19 NMR/MRI signals were employed to sense the activity of these two important enzymes in vitro and in cell lysates for the first time. We anticipate that our new F-19 NMR/magnetic, resonance imaging (MRI) method would facilitate pharmaceutical researchers to screen new inhibitors for these two enzymes without steric hindrance.
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