A host–guest based fluorescence sensor array can sense small differences in protein structure. The combination of three cavitand hosts and two fluorophores to form a 4-component array is sufficient to fully discriminate five structurally similar Ig protein isotypes. The array can be applied to recognize Ig deficiencies in serum, when combined with a Protein L-based extraction process, allowing analysis of immunodeficiency in a simpler, lower cost manner than tests that require multiple specific antibodies.
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The effects on the molecular recognition properties of water-soluble deep cavitand hosts upon embedding them in phosphocholine lipid bilayer environments have been studied by 2D NMR experiments. By employing suitable guests containing 19 F or 13 C nuclei that can be encapsulated inside the host, 2D EXSY NMR experiments can be used to analyze and compare the in/out guest exchange rates in aqueous solution, isotropically tumbling micelles, or magnetically ordered bicelles. These analyses show that embedding the deep cavitands in lipid bilayers slows the guest exchange rate, due to the lipids acting as a “compression sleeve” around the host, restricting guest egress. This effect also enhances guest conformations in the host that are not observed in free solution, such as axial cyclohexane conformers and ketone hydrates.more » « less
