In this work, porphyrinic metal-organic frameworks (MOFs) with longitudinal Pt deposition were developed for the inspired establishment of opto/catalytic adjuvants referenced for a dual-path glycoprotein assay. In the compositional cooperation, porphyrinic MOFs were synthesized through Zr oxoclusters and polytopic porphyrin ligands into a benchmark template (PCN-222), followed by catalytic Pt nanowire deposition (PtNW@PCN-222). As for signal reflection, the fluorogenic species (i.e., resazurin and amplex red) were integrated into zeolitic imidazolate framework-8 (ZIF-8) via epitaxial shell growth to guide lectin integration. The specific performance toward glycoprotein recognition was guaranteed by both antibody-antigen interaction as well as glycan epitope binding through lectin affinity, and the signal response was initiated by textural decomposition of the ZIF-8 skeleton in a controllable manner. On one hand, PtNW@PCN-222 can function as the catalytic adjuvant to exert the fluorogenic reactions: a reductive N-deoxygenation of resazurin and an oxidative N-deacetylation of amplex red, in which both the redox reactions generated the fluorescent species of resorufin products. On the other hand, PtNW@PCN-222 with endogenous periodical arrangement of porphyrin ligands can be tailored as an optical adjuvant for reporting signal reference. For benefits, the comprehensive functions leaned on the catalytic performance and optical reference property from PtNW@PCN-222 can be harvested for a ratiometric glycoprotein assay. Besides, due to the variant catalytic converter of PtNW@PCN-222 involved in the two fluorogenic reactions, the proposed glycoprotein assay exhibited a range of 0.03-3 nM with a detection limit of 7.91 pM in the reductive pathway, and showed a linear range from 0.06 to 10 nM with a detection limit of 21.64 pM in the oxidative pathway. Collectively, our proposed glycoprotein assay may provide a new thought in opto/catalytic MOF adjuvant-empowered ratiometric sensing in the dual-path reflection manner, which may also reinforce the accurate detection capability for the glycoprotein assay.
Yang et al. (Wed,) studied this question.