Protein and small molecule recognition properties of deep cavitands in a supported lipid membrane determined by calcination-enhanced SPR spectroscopy.
Protein and small molecule recognition properties of deep cavitands in a supported lipid membrane determined by calcination-enhanced SPR spectroscopy.
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DOI:
10.1021/ja102252d
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发表时间:
2010-08-04
影响因子:
15
通讯作者:
Hooley, Richard J.
中科院分区:
文献类型:
--
作者:
Liu, Ying;Liao, Puhong;Cheng, Quan;Hooley, Richard J.
This report details the incorporation of a water-soluble deep cavitand into a membrane bilayer assembled onto a nanoglassified surface for study of molecular recognition in a membrane-mimicking setting. The cavitand retains its host properties, and real-time analysis of the host:guest properties of the membrane:cavitand complex via surface plasmon resonance and fluorescence microscopy is described. The host shows selectivity for choline-derived substrates, and no competitive incorporation of substrate is observed in the membrane bilayer. A variety of trimethylammonium-derived substrates are suitable guests, displaying binding affinities in a millimolar range. The membrane:cavitand:guest complexes can be subsequently used to capture NeutrAvidin protein at the membrane surface if a biotin-derived guest molecule is used. The surface coverage of NeutrAvidin is affected by the spacer used to derivatize the biotin. Increased distance from the bilayer allows a higher concentration of protein to be immobilized, suggesting a diminishing detrimental steric effect when the binding event is shifted away from the surface.
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