{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,10,3]],"date-time":"2026-10-03T07:38:45Z","timestamp":1791013125863,"version":"4.1.0"},"reference-count":46,"publisher":"Wiley","issue":"17","license":[{"start":{"date-parts":[[2007,8,3]],"date-time":"2007-08-03T00:00:00Z","timestamp":1186099200000},"content-version":"vor","delay-in-days":0,"URL":"http:\/\/onlinelibrary.wiley.com\/termsAndConditions#vor"}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["Electrophoresis"],"published-print":{"date-parts":[[2007,9]]},"abstract":"<jats:title>Abstract<\/jats:title><jats:p>A method for creating an immobilized capillary acetylcholinesterase (AChE) reactor based on a layer\u2010by\u2010layer (LBL) assembly for inhibitor screening is described. The unique capillary AChE reactor was easily prepared by the instrument in three steps: first, a 0.5\u2005cm long plug of a solution of the cationic polyelectrolyte polydiallyldimethylammonium (PDDA) was injected into the capillary to produce a positively charged coating on the surface of the capillary; subsequently, the enzyme solution with the same plug length was injected into the capillary and incubated for 10\u2005min to immobilize the enzyme on the capillary wall <jats:italic>via<\/jats:italic> electrostatic interaction; third, PDDA solution with the same plug length was injected again into the capillary to cover the immobilized enzyme by forming PDDA\u2013AChE\u2013PDDA sandwich\u2010like structure. The enzyme reactor can be easily renewed after removing the immobilized enzyme by flushing the column with 1\u2005M NaCl solution. Activity of the immobilized enzyme can be assayed simply by carrying out an electrophoretic separation, <jats:italic>i.e.<\/jats:italic>, the substrate solution was injected and incubated for a short time, followed by applying a voltage to separate the product from the unreacted substrate. The measured peak area of the product then represented the enzyme activity. For enzyme inhibitor screening, the mixture solution of the substrate and the inhibitor was injected and assayed the reduction of the enzyme activity. The immobilized enzyme could withstand 100 consecutive assays by only losing 10% activity. The reproducibility in terms of time\u2010to\u2010time, day\u2010to\u2010day, and batch\u2010to\u2010batch was measured with RSD% less than 4.7%. Furthermore, the screening system was validated by a known inhibitor. Finally, screening a small compound library containing four known AChE inhibitors and 42 natural extracts was demonstrated, and species with inhibition activity can be straightforwardly identified with the system.<\/jats:p>","DOI":"10.1002\/elps.200700061","type":"journal-article","created":{"date-parts":[[2007,8,3]],"date-time":"2007-08-03T05:19:52Z","timestamp":1186118392000},"page":"2981-2987","source":"Crossref","is-referenced-by-count":62,"title":["Immobilized capillary enzyme reactor based on layer\u2010by\u2010layer assembling acetylcholinesterase for inhibitor screening by CE"],"prefix":"10.1002","volume":"28","author":[{"given":"Zhongmei","family":"Tang","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Tongdan","family":"Wang","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Jingwu","family":"Kang","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"311","published-online":{"date-parts":[[2007,8,27]]},"reference":[{"key":"e_1_2_1_2_2","doi-asserted-by":"publisher","DOI":"10.1002\/anie.200585328"},{"key":"e_1_2_1_3_2","doi-asserted-by":"publisher","DOI":"10.1126\/science.1095920"},{"key":"e_1_2_1_4_2","doi-asserted-by":"publisher","DOI":"10.1111\/j.1365-2125.1989.tb03475.x"},{"key":"e_1_2_1_5_2","doi-asserted-by":"publisher","DOI":"10.1016\/j.jchromb.2004.07.008"},{"key":"e_1_2_1_6_2","doi-asserted-by":"publisher","DOI":"10.1002\/cbic.200400211"},{"key":"e_1_2_1_7_2","doi-asserted-by":"publisher","DOI":"10.1016\/j.drudis.2006.05.002"},{"key":"e_1_2_1_8_2","first-page":"175","volume":"797","author":"Burns K. 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