fig12

Figure 12. (A) Synthetic route of Fe₃O₄@Thio-COF@Au@GSH; (B) Workflow for the enrichment of glycopeptides and phosphopeptides in standard samples by Fe₃O₄@Thio-COF@Au@GSH individually; (C) Workflow of the consecutive enrichment of exosomes and exosomal glycopeptides/phosphopeptides from urine samples using Fe₃O₄@Thio-COF@Au@GSH; (D) Calculated electron density mapped with the electrostatic potential of GSH/phosphate head group; (E) Possible interaction model between GSH and the phosphate head group. Hydrogen bonds are represented by blue dashed lines; (F) Protein–protein interaction network of the identified 42 proteins with the co-existence of glycosylation and phosphorylation; (G) Preparation diagram of ferrocene COF; (H and I) TEM (H) and SEM (I) images of FE-1; (J) Mass spectrum of eluent obtained by enriching glycopeptides in IgG enzymatic hydrolysate with FE-1 COF material; (K) Mass spectrum of eluent obtained by enriching phosphopeptides in α-casein enzymatic hydrolysate with FE-1 COF material. (A-F) are reprinted with permission from Ref^[139], Copyright © 2022 by Royal Society of Chemistry. (G-K) are reproduced with permission from Ref.^[140], Copyright © 2024 by Multidisciplinary Digital Publishing Institute. Thio-COF: Thioether-functionalized covalent organic framework; GSH: glutathione; TEM: transmission electron microscopy; SEM: scanning electron microscope; IgG: immunoglobulin G.