caa a22 4500 445803304 CHVBK 20180317145148.0 cr unu---uuuuu 170323e20111001xx s 000 0 eng 10.1007/s10337-011-2102-7 doi (NATIONALLICENCE)springer-10.1007/s10337-011-2102-7 Monoamine Oxidase Inhibitor Screening by Proteoliposome Capillary Electrophoresis [Elektronische Daten] [Bing Li, Xuefei Lv, Hong Qing, Lina Geng, Yulin Deng] In this study, a new strategy for screening of enzyme inhibitors based on the interaction between enzyme and substrate was established. The bioactive proteoliposome reconstituted by monoamine oxidase (MAO) and liposome was added in the running buffers of capillary electrophoresis (CE) as pseudostationary phase to simulate the interaction between MAO and its substrate kynuramine (Kyn). The results showed that the relative migration time ratio (RMTR) of Kyn decreased obviously with increase of the proteoliposome, indicating strong interaction between proteoliposome and Kyn. After adding MAO inhibitors into the running buffers containing proteoliposome, the decline of the RMTR value of Kyn became slower. This occurred because MAO was inhibited to some degree by the inhibitors, weakening the interaction between MAO and Kyn. However, adding compounds which do not inhibit MAO activity into the running buffers did not affect the RMTR of Kyn obviously. The results obtained demonstrate that the method developed could characterize the inhibition of MAO inhibitors. Compared with traditional inhibitor screening methods, it does not need incubation outside the column to complete the enzyme catalytic reaction, so analysis is faster and less sample is consumed. With further development, the method might be chosen as a useful tool for screening of membrane protein inhibitors and identification of proteins associated with various diseases. Springer-Verlag, 2011 Capillary electrophoresis nationallicence Proteoliposome nationallicence Kynuramine nationallicence Monoamine oxidase nationallicence Inhibitor nationallicence Li Bing School of Life Science, Beijing Institute of Technology, 100081, Beijing, China aut Lv Xuefei School of Life Science, Beijing Institute of Technology, 100081, Beijing, China aut Qing Hong School of Life Science, Beijing Institute of Technology, 100081, Beijing, China aut Geng Lina School of Life Science, Beijing Institute of Technology, 100081, Beijing, China aut Deng Yulin School of Life Science, Beijing Institute of Technology, 100081, Beijing, China aut Chromatographia Springer-Verlag 74/7-8(2011-10-01), 619-624 0009-5893 74:7-8<619 2011 74 10337 https://doi.org/10.1007/s10337-011-2102-7 text/html Onlinezugriff via DOI 1 research-article jats NATIONALLICENCE 856 40 https://doi.org/10.1007/s10337-011-2102-7 text/html Onlinezugriff via DOI NATIONALLICENCE 700 1- Li Bing School of Life Science, Beijing Institute of Technology, 100081, Beijing, China aut NATIONALLICENCE 700 1- Lv Xuefei School of Life Science, Beijing Institute of Technology, 100081, Beijing, China aut NATIONALLICENCE 700 1- Qing Hong School of Life Science, Beijing Institute of Technology, 100081, Beijing, China aut NATIONALLICENCE 700 1- Geng Lina School of Life Science, Beijing Institute of Technology, 100081, Beijing, China aut NATIONALLICENCE 700 1- Deng Yulin School of Life Science, Beijing Institute of Technology, 100081, Beijing, China aut NATIONALLICENCE 773 0- Chromatographia Springer-Verlag 74/7-8(2011-10-01), 619-624 0009-5893 74:7-8<619 2011 74 10337 Metadata rights reserved Springer special CC-BY-NC licence nationallicence BK010053 XK010053 XK010000 NATIONALLICENCE NATIONALLICENCE NL-springer