التفاصيل البيبلوغرافية
| العنوان: |
Fluorogenic and chromogenic detection of carboxypeptidase Y with a nonpeptide-based small-molecule probe. |
| المؤلفون: |
Xiong, Hao1,2, Yang, Jia-Qian1,2, Kang, Wei-Ming1,2, Wu, Feng-Xu1,2, Zuo, Jia-Li1,2, Zhou, Zi-Yu1,2, Yang, Wen-Chao1,2 tomyang@mail.ccnu.edu.cn, Yang, Guang-Fu1,2,3 gfyang@mail.ccnu.edu.cn |
| المصدر: |
Sensors & Actuators B: Chemical. Sep2018, Vol. 269, p127-134. 8p. |
| مصطلحات موضوعية: |
*CARBOXYPEPTIDASES, *CHEMICAL synthesis, *POLYPEPTIDES, *AMINO acid sequence, *FLUORESCENT probes, *HYDROLYSIS |
| مستخلص: |
Carboxypeptidase Y (CPY) is a vital enzyme with many well-known biological significances, such as determination of amino acid sequences and biosynthesis of polypeptides. Herein we developed a nonpeptide-based fluorescent probe to sense CPY activity accurately and successfully applied it to the inhibitory study. Based on the organic synthesis and comprehensive characterization, the refined probe CPY-P3 displayed excellent specificity towards CPY and exhibited over 400-fold enhancement of fluorescence intensity upon the hydrolysis of CPY. Compared with the commonly used peptide-based fluorescent substrate ( Suc-IIW-AMC ), CPY-P3 showed about 12-fold higher binding affinity and comparable catalytical efficiency for CPY. Moreover, CPY-P3 was successfully applied in CPY inhibitor characterization. To our knowledge, CPY-P3 is the first nonpeptide-based small-molecule fluorescent probe for the time-course CPY activity detection. Meanwhile, the generation of kelly color makes the detection directly visible without any complicated device. In all, this small-molecule probe should be a potentially useful tool in understanding the roles of CPY in protein sequencing and engineering, as well as the drug discovery of CPY-related diseases. [ABSTRACT FROM AUTHOR] |
| قاعدة البيانات: |
Academic Search Index |
