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A Kinetic Fluorescence-based Ca2+ Mobilization Assay to Identify G Protein-coupled Receptor Agonists, Antagonists, and Allosteric Modulators
Published on: February 20, 2018
A study of allosteric binding behaviour of a 1,3-alternate thiacalix[4]arene-based receptor using fluorescence signal
Hirotsugu Tomiyasu1, Cheng-Cheng Jin, Xin-Long Ni
1Department of Applied Chemistry, Faculty of Science and Engineering, Saga University, Honjo-machi 1, Saga 840-8502, Japan. yamatot@cc.saga-u.ac.jp.
Abstract:
A novel heteroditopic thiacalix[4]arene receptor L possessing 1,3-alternate conformation, which contains two pyrene moieties attached to the lower rim via urea linkages together with a crown ether moiety appended at the opposite side of the thiacalix[4]arene cavity, has been synthesized. The complexation behaviour of receptor L was studied by means of fluorescence spectra and (1)H NMR titration experiments in the presence of K(+) ions and a variety of other anions. The results suggested that receptor L can complex efficiently via the urea cavity or the crown ether moiety, and a positive/negative allosteric effect operating in receptor L was observed.
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