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 (A beta 1-42) 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, ultrahigh specific surface (2552 m(2)/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 A beta 1-42, 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 A beta 1-42 in human serum by using C-peptide as an internal standard, which exhibited low limit of detection (LOD, 0.2 fmol/mu L), and satisfactory recovery. This work provides an alternative solution for enrichment of biomarkers and also offers the potential applications of COFs in clinical analysis (c) 2022 Published by Elsevier B.V. on behalf of Chinese Chemical Society and Institute of Materia Medica, Chinese Academy of Medical Sciences.