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• W2072770623 abstract "This article provides an overview of our recent studies on developing functionalized lipid bilayer membranes, on which enzymatic activity was controlled by a molecular switch through connection of molecular recognition. A water-soluble enzyme, such as lactate dehydrogenase, was immobilized noncovalently on the lipid vesicular surface maintaining the catalytic activity. Various types of molecular switches capable of performing as ditopic receptors for an organic signal molecule and a metal ion were prepared and embedded in the lipid membrane. The resulting supramolecular assemblies exhibited the functions of molecular devices triggered by an input signal, which synchronize the enzymatic activity with the recognition of the molecular switch by using a metal ion as a mediator species between the enzyme and the molecular switch. The cationic bilayer membrane formed with the synthetic peptide lipids or the Cerasome-forming lipids is an effective platform for such molecular devices." @default.
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• W2072770623 date "2005-01-01" @default.
• W2072770623 modified "2023-09-27" @default.
• W2072770623 title "Switching of Enzymatic Activity through Functional Connection of Molecular Recognition on Lipid Bilayer Membranes" @default.
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• W2072770623 doi "https://doi.org/10.1080/10610270412331329023" @default.
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