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An Air‐Supported Liquid Crystal System for Real‐Time and Label‐Free Characterization of Phospholipases and Their Inhibitors
Author(s) -
Hartono Deny,
Bi Xinyan,
Yang KunLin,
Yung LinYue Lanry
Publication year - 2008
Publication title -
advanced functional materials
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 6.069
H-Index - 322
eISSN - 1616-3028
pISSN - 1616-301X
DOI - 10.1002/adfm.200800424
Subject(s) - phospholipase , phospholipase c , phospholipase d , materials science , phospholipid , liquid crystal , monolayer , phospholipase a , enzyme , aqueous solution , phosphoinositide phospholipase c , hydrolysis , chromatography , biophysics , phospholipase a2 , organic chemistry , biochemistry , nanotechnology , chemistry , biology , optoelectronics , membrane
A new air‐supported liquid crystal (LC) system for analyzing interfacial phenomena that occur based on the molecular interaction between LCs and adsorbed molecules of interest at the aqueous/LC interface is reported. Compared with existing LC‐based detection systems, the miniature system reported here requires less sample and involves simpler preparation. Using this system, the enzymatic hydrolysis of various phospholipases such as phospholipase A 2 (PLA 2 ), phospholipase C (PLC) and phospholipase D (PLD) are characterized. The hydrolysis of phospholipid monolayers self‐assembled at aqueous/LC interface induces an orientational response from the LCs. As a result, an optical signal that reflects the spatial and temporal distribution of phospholipids during the enzymatic reaction can be generated in a real‐time manner. When well‐known phospholipase inhibitors are introduced together with respective phospholipases, no orientational response of LCs is observed. In the case of inhibitors MJ33 and compound 48/80, cross‐inhibitions among phospholipases are also observed. This work demonstrates that the air‐supported LC system provides a facile label‐free assay for characterizing phospholipase activities and for screening enzyme inhibitors. It could potentially be useful for different high throughput and cost‐effective enzyme screening assays.