Integración inspirada en células naturales de moléculas reactivas redox en MOFs jerárquicos cosechados para el ensayo...

Natural cell systems with multiple isolated compartments possess controllable signal transduction pathways, which can segregate a series of complex substances and confine them from each other to allow for feedback-driven reactions. By biomimicking the ingenuity of cell systems, we herein designed spatially compact metal-organic frameworks (MOFs) as a hierarchical host for complex substances at isolated locations for the development of reaction pathway-regulated glycoprotein assay. The well-defined zeolitic imidazolate framework-8 (ZIF-8) matrices were fabricated via epitaxial growth to organize the multishelled integration of multiple guest substances including redox reactant substrates (i.e., resazurin and amplex red) and Pt-shelled Au (AuPt) entities. In addition, the micropore nature and enclosed space of the ZIF-8 matrix can prohibit the surpassed contact between fluorogenic substrates and catalytic AuPt converters, inherently, while the immediate signal generator pattern can be harvested through textural collapse of the ZIF-8 skeleton in a controllable manner. Our proposed glycoprotein assay can be conducted with on-demand redox reactions for signal generators: a reductive N-deoxygenation of resazurin and an oxidative N-deacetylation of amplex red, respectively. Due to the distinct catalytic behavior of AuPt converters involved in the fluorogenic redox reactions, the detection limit of the reaction pathway-regulated glycoprotein assay can reach 14.27 pM for the reductive N-deoxygenation reaction and 71.63 pM for the oxidative N-deacetylation reaction, respectively. Collectively, our proposed method may offer an innovative inspiration of reaction pathway-regulated glycoprotein assay, and it can also be adapted for rational substitution of substrate molecules to broaden its signal reflections in versatile glycoprotein analysis.