Abstract
Here, we present a novel method for reversibly regulating enzyme activity by caging an enzyme into a pH-responsive DNA-based tetrahedron nanostructure. pH-dependent opening/closing of the DNA cage was verified by measuring fluorescence resonance energy transfer between two vertex corners of the tetrahedron. The position of the covalent enzyme attachment in DNA was carefully chosen such that the attached enzyme faced inward the DNA cage. Both proteinase K protection assay and single-molecule based pull-down assay showed that the encapsulated enzyme were exposed to either proteinase K or target antibody by pH-dependent opening of DNA cage. Remarkably, we found that the caging/uncaging process were reversible, implying that enzyme activity toward relatively larger substrates than DNA cage can be reversibly regulated. Considering that the DNA cage is widely used as a delivery carrier, our method can be further extended to reversibly regulate cell function by pH-dependent activity control of delivered enzyme.
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