Abstract
A complex between an anionic polythiophene derivative (PT-COO(-)) and a cationic surfactant, myristoylcholine, has been prepared and applied to be colorimetric probe for acetylcholinesterase (AChE) assays. The complex formation process, AChE activity assay and inhibitor screening has been studied by absorption spectroscopy. It was confirmed that the introduction of myristoylcholine into PT-COO(-) phosphate buffer solution resulted in the disassembly of PT-COO(-) aggregates, and further addition of AChE into the above solution led to the reassembly of PT-COO(-) due to the catalyzed hydrolysis of myristoylcholine and the collapse of the complex. The colorimetric assay for AChE can be readily realized with the concentration of AChE as low as 0.2 U/mL. The results also demonstrate that the colorimetric approach can be applied for screening inhibitors of AChE.
Sign-in/Register to access full text options 
Talk to us
Join us for a 30 min session where you can share your feedback and ask us any queries you have
Schedule a callDisclaimer: All third-party content on this website/platform is and will remain the property of their respective owners and is provided on "as is" basis without any warranties, express or implied. Use of third-party content does not indicate any affiliation, sponsorship with or endorsement by them. Any references to third-party content is to identify the corresponding services and shall be considered fair use under The CopyrightLaw.
