Copper(II) ions-immobilized virus-like hollow covalent organic frameworks for highly efficient capture and sensitive analysis of amyloid beta-peptide 1–42 by MALDI-MS

Amyloid beta-peptide 1–42 (Aβ1–42) is one of the biomarkers of Alzheimer's disease, and its selective capture and quantitative detection are important for diagnosis and treatment of Alzheimer's disease. Herein, copper(II) ions-immobilized virus-like hollow covalent organic frameworks (V-HCOFs@Cu2+) were synthesized by a facile approach. The as-prepared V-HCOFs@Cu2+ showed unique morphology, ultra-high specific surface (2552 m2/g), uniform mesoporous structure (3.2 nm), superior chemical stability and abundant binding sites. Based on these excellent properties, the V-HCOFs@Cu2+ could be adopted as an ideal enrichment probe for highly efficient capture of Aβ1–42, exhibiting high adsorption capacity (320 mg/g), and fast adsorption equilibration time (3 min). In addition, an attractive approach of the V-HCOFs@Cu2+-based matrix-assisted laser desorption/ionization mass spectrometry (MALDI-MS) was developed for the rapid screening and quantitative analysis of Aβ1–42 in human serum by using C-peptide as an internal standard, which exhibited low limit of detection (LOD, 0.2 fmol/µL), and satisfactory recovery. This work provides an alternative solution for enrichment of biomarkers and also offers the potential applications of COFs in clinical analysis [Display omitted] V-HCOFs@Cu2+ were synthesized via a facile approach at room temperature and applied as an adsorption probe for selective capture and quantitative analysis of Aβ1–42 from human serum by MALDI-MS.