Bioinspired Spatial Compartment of Substrate Molecules and Catalytic Counting Entities in Hierarchical MOFs Initiated...

Living cell systems possess multiple isolated compartments that can spatially confine complex substances and shield them from each other to allow for feedback reactions. In this work, a bioinspired design of metal-organic frameworks (MOFs) with well-defined multishelled matrices was fabricated as a hierarchical host for multiple guest substances including fluorogenic molecules and catalytic nanoparticles (NPs) at the separated locations for the development of a dual-mode glycoprotein assay. The multispatial-compartmental zeolitic imidazolate framework-8 (ZIF-8) constituents were synthesized via epitaxial shell-by-shell overgrowth to guide the integration and spatial organization of host guests. The specific property toward glycoprotein recognition was guaranteed by both the antibody-antigen recognition and covalent bonding through boronate-glycan affinity, and the immediate signal responses were initiated by textural collapse of the ZIF-8 integrity. In addition, the inner micropore and the enclosed space of ZIF-8 can avoid the surpassed contact between molecular substances and catalytic entities, inherently. Furthermore, multishelled ZIF-8 can function as a hierarchical matrix for hosting abundant fluorogenic substrates and a large number of catalytic Pt-shelled Au (AuPt) NPs, which can signify its signal amplification means, while upon the stimuli-responsive framework collapse, the signal generators can be harvested in the on-demand manner. Besides, endowing Pt shells on inert plasmonic NPs can not only mimic peroxidase-like catalytic behavior involved in a fluorogenic catalytic reaction to generate fluorescence signals but also function as scattering signal reporters, which can also signify the dynamic light scattering output signals. Collectively, our proposed method may provide a new thought in combining the well-defined multishelled MOF matrices for dual-signal generators in a stimuli-responsive manner, which can also reinforce the accurate detection capability for the glycoprotein assay.