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A designable aminophenylboronic acid functionalized magnetic Fe(3)O(4)/ZIF-8/APBA for specific recognition of glycoproteins and glycopeptides

We fabricated a novel aminophenylboronic acid functionalized magnetic Fe(3)O(4)/zeolitic imidazolate framework-8/APBA (denoted as Fe(3)O(4)/ZIF-8/APBA). First, Fe(3)O(4) was coated by zeolitic imidazolate framework-8 (denoted as Fe(3)O(4)/ZIF-8) using the hydrothermal method. Next, the phenylboronic...

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Detalles Bibliográficos
Autores principales: Li, Shanshan, Li, Dongyan, Sun, Long, Yao, Yuewei, Yao, Cheng
Formato: Online Artículo Texto
Lenguaje:English
Publicado: The Royal Society of Chemistry 2018
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9078308/
https://www.ncbi.nlm.nih.gov/pubmed/35540317
http://dx.doi.org/10.1039/c7ra12054k
Descripción
Sumario:We fabricated a novel aminophenylboronic acid functionalized magnetic Fe(3)O(4)/zeolitic imidazolate framework-8/APBA (denoted as Fe(3)O(4)/ZIF-8/APBA). First, Fe(3)O(4) was coated by zeolitic imidazolate framework-8 (denoted as Fe(3)O(4)/ZIF-8) using the hydrothermal method. Next, the phenylboronic acid functionalized triethoxysilane reagent was synthesized by 3-aminophenylboronic acid and 3-isocyanatopropyltriethoxysilane, which was modified on the surface of the Fe(3)O(4)/ZIF-8 nanocomposite through the sol–gel technique and electrostatic interaction as well as π–π stacking interaction. The synthetic Fe(3)O(4)/ZIF-8/APBA exhibited high adsorption capacity and good specificity toward glycoproteins. Moreover, the Fe(3)O(4)/ZIF-8/APBA possessed high saturation magnetization (51.41 emu g(−1)) and achieved better separation in the presence of an external magnetic field. Above all, the as-designed Fe(3)O(4)/ZIF-8/APBA was successfully used to capture glycoproteins and identify the horseradish peroxidase (HRP) tryptic digest. This study provides a facile strategy to embellish the aminophenylboronic acid onto the nanocomposite substrate and develop a new material for the specific recognition and enrichment of glycoproteins and low-abundance glycopeptides in proteomics research.