Core-shell structured magnetic covalent organic frameworks (FeO@COFs) were synthesized via a facile approach at room temperature. Combining the advantages of high porosity, magnetic responsiveness, chemical stability and selectivity, FeO@COFs can serve as an ideal absorbent for the highly efficient enrichment of peptides and the simultaneous exclusion of proteins from complex biological samples.

No abstract

Core–shell structured Fe3O4@TbBd composite nanospheres were synthesised using a facile approach and successfully applied for selective enrichment of peptides with simultaneous exclusion of proteins.

In the past few years, the immobilization of biomolecules on hybrid nanoflowers and metal–organic frameworks (MOFs) via self-assembly synthesis has received much attention due to its superior advantages.

Chemical modification of covalent organic frameworks (COFs) is indispensable for integrating functionalities of greater complexity and accessing advanced COF materials suitable for more potential applications. Reported here is a novel strategy for fabricating controllable core–shell structured Zr4+-immobilized magnetic COFs (MCNC@COF@Zr4+) composed of a high-magnetic-response magnetic colloid nanocrystal cluster (MCNC) core, Zr4+ ion-functionalized two-dimensional COFs as the shell by sequential postsynthetic functionalization and, for the first time, the application of the MCNC@COF@Zr4+ composites for efficient and selective enrichment of phosphopeptides. The as-prepared MCNC@COF@Zr4+ composites possess regular porosity with large surface areas, high Zr4+ loading amount, strong magnetic responsiveness, and good thermal/chemical stability, which can serve as an ideal adsorbent for selective enrichment of phosphopeptides and simultaneous size exclusion of biomacromolecules, such as proteins. The high detection sensitivity (10 fmol) together with the excellent recovery of phosphopeptides is also obtained. These outstanding features suggest that the MCNC@COF@Zr4+ composites are of great benefit for pretreatment prior to mass spectrometry analysis of phosphopeptides. In addition, the performance of the developed approach in selective enrichment of phosphopeptides from the tryptic digests of defatted milk and directly specific capture of endogenous phosphopeptides from human serum gives powerful proof for its high selectivity and effectiveness in identifying the low-abundance phosphopeptides from complicated biological samples. This study not only provides a strategy for versatile functionalization of magnetic COFs but also opens a new avenue in their use in phosphoproteome analysis.

A facile approach was developed for one-pot synthesis of trypsin-based magnetic ZIF-8, which could be applied as an immobilized enzyme microreactor for rapid digestion of proteins.