title: Zirconium arsenate-modified magnetic nanoparticles: preparation, characterization and application to the enrichment of phosphopeptides.
abstract: Phosphorylation, one of the most important post-translational modifications of protein, plays a crucial role in a large number of biological processes. Large-scale identification of protein phosphorylation by mass spectrometry is still a challenging task because of the low abundance of phosphopeptides and sub-stoichiometry of phosphorylation. In this work, a novel strategy based on the specific affinity of zirconium arsenate to the phosphate group has been developed for the effective enrichment of phosphopeptides. Zirconium arsenate-modified magnetic nanoparticles (ZrAs-Fe(3)O(4)@SiO(2)) were prepared by covalent immobilization of zirconium arsenate on Fe(3)O(4)@SiO(2) magnetic nanoparticles under mild conditions, and characterized by transmission electron microscope (TEM), Fourier transform infrared (FT-IR) spectroscopy, energy dispersive X-ray spectroscopy (EDX) and vibrating sample magnetometer (VSM). The prepared ZrAs-Fe(3)O(4)@SiO(2) was applied for the selective enrichment of phosphopeptides from the digestion mixture of phosphoproteins and bovine serum albumin (BSA). Our results demonstrated that the ZrAs-Fe(3)O(4)@SiO(2) magnetic nanoparticles possess higher selectivity for phosphopeptides and better capture capability towards multiply-phosphorylated peptides than commercial zirconium dioxide (ZrO(2)), which has been widely employed for the enrichment of phosphopeptides. In addition, endogenous phosphopeptides from human serum can be effectively captured by ZrAs-Fe(3)O(4)@SiO(2) magnetic nanoparticles. It is the first report, to the best of our knowledge, in which the zirconium arsenate-modified magnetic nanoparticles were successfully applied to the enrichment of phosphopeptides, which offers the potential application of this new material in phosphoproteomics study.
authors.affiliation: Key Laboratory of Analytical Chemistry for Biology and Medicine (Ministry of Education), Department of Chemistry, Wuhan University, Wuhan 430072, PR China.
authors.forename: Xiao-Shui
authors.initials: XS
authors.lastname: Li
authors.forename: Li-Dan
authors.initials: LD
authors.lastname: Xu
authors.forename: Gang-Tian
authors.initials: GT
authors.lastname: Zhu
authors.forename: Bi-Feng
authors.initials: BF
authors.lastname: Yuan
authors.forename: Yu-Qi
authors.initials: YQ
authors.lastname: Feng
mesh_terms: D001149:Arsenates / Q000737:chemistry; D001798:Blood Proteins / Q000032:analysis* / Q000737:chemistry / Q000378:metabolism; D006801:Humans; D058185:Magnetite Nanoparticles; D013058:Mass Spectrometry / Q000379:methods; D010748:Phosphopeptides / Q000032:analysis* / Q000737:chemistry; D010766:Phosphorylation; D011506:Proteins / Q000032:analysis* / Q000737:chemistry / Q000378:metabolism; D015040:Zirconium / Q000737:chemistry
chemical_list: D001149:Arsenates; D001798:Blood Proteins; D058185:Magnetite Nanoparticles; D010748:Phosphopeptides; D011506:Proteins; D015040:Zirconium; C025657:arsenic acid