Access to both protein and metabolite biomarker information
in
biospecimens from trace samples remains a significant challenge, and
it is necessary to separate proteins and metabolites before analysis.
In this work, the Fe3O4@SiO2@Proteins@Metal-polyphenol
network (MPN) was successfully constructed and applied to separate
metabolites and proteins. Tannic acid (TA) and Cu2+ were
involved in the synthesis of MPN because of rapid degradation and
maintaining the assay performance of proteins. There are a variety
of interactions between TA and proteins, including hydrogen-bonding,
hydrophobic, and ionic interactions. Moreover, benefiting from the
small molecule permeability and surface adherence of MPN, proteins
were encapsulated and immobilized on the surface of substrates with
the growth of MPN. At the same time, endogenous metabolites remained
dispersed in the supernatant. In the model sample and real biospecimen
cases, the protein biomarkers (e.g., carcinoembryonic antigen and
alanine aminotransferase) were encapsulated on the surface of Fe3O4@SiO2, which allowed the isolation
of proteins from the original matrix, as well as release and analysis
in a short time. Meanwhile, the metabolites in the produced supernatant
were analyzed by LC-MS/MS. By the self-assembly and disassembly of
MPN, the group differences of proteins and metabolites between physiological
and pathological biospecimens are correctly characterized without
multisampling. Overall, an MPN-mediated separation strategy of biomarkers
was proposed, and MPN facilitated a “two birds with one stone”
approach, where the proteins were encapsulated and immobilized in
the precipitation while endogenous metabolites distributed in the
produced supernatant, opening a new chapter in the application of
MPNs.
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