التفاصيل البيبلوغرافية
| العنوان: |
Turn-on Coumarin Precursor: From Hydrazine Sensor to Covalent Inhibition and Fluorescence Detection of Rabbit Muscle Aldolase. |
| المؤلفون: |
Amer, Sara1 (AUTHOR), Miles, Uri1 (AUTHOR), Firer, Michael2,3 (AUTHOR) firer@ariel.ac.il, Grynszpan, Flavio1 (AUTHOR) flaviog@ariel.ac.il |
| المصدر: |
Molecules. May2024, Vol. 29 Issue 10, p2175. 16p. |
| مصطلحات موضوعية: |
*HYDRAZINE, *HYDRAZINES, *FLUORESCENCE, *RABBITS, *DETECTORS, *BINDING sites, *HYDRAZINE derivatives, *COUMARINS |
| مستخلص: |
Hydrazine, a highly toxic compound, demands sensitive and selective detection methods. Building upon our previous studies with pre-coumarin OFF–ON sensors for fluoride anions, we extended our strategy to hydrazine sensing by adapting phenol protecting groups (propionate, levulinate, and γ-bromobutanoate) to our pre-coumarin scaffold. These probes reacted with hydrazine, yielding a fluorescent signal with low micromolar limits of detection. Mechanistic studies revealed that hydrazine deprotection may be outperformed by a retro-Knoevenagel reaction, where hydrazine acts as a nucleophile and a base yielding a fluorescent diimide compound (6,6′-((1E,1′E)-hydrazine-1,2diylidenebis(methaneylylidene))bis(3(diethylamino)phenol, 7). Additionally, our pre-coumarins unexpectedly reacted with primary amines, generating a fluorescent signal corresponding to phenol deprotection followed by cyclization and coumarin formation. The potential of compound 3 as a theranostic Turn-On coumarin precursor was also explored. We propose that its reaction with ALDOA produced a γ-lactam, blocking the catalytic nucleophilic amine in the enzyme's binding site. The cleavage of the ester group in compound 3 induced the formation of fluorescent coumarin 4. This fluorescent signal was proportional to ALDOA concentration, demonstrating the potential of compound 3 for future theranostic studies in vivo. [ABSTRACT FROM AUTHOR] |
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