Ti(IV) carrying polydopamine-coated, monodisperse-porous SiO2 microspheres with stable magnetic properties for highly selective enrichment of phosphopeptides


Salimi K., USTA D. Y. , ÇELİKBIÇAK Ö., PINAR A., SALİH B., Tuncel A.

COLLOIDS AND SURFACES B-BIOINTERFACES, cilt.153, ss.280-290, 2017 (SCI İndekslerine Giren Dergi)

  • Cilt numarası: 153
  • Basım Tarihi: 2017
  • Doi Numarası: 10.1016/j.colsurfb.2017.02.028
  • Dergi Adı: COLLOIDS AND SURFACES B-BIOINTERFACES
  • Sayfa Sayısı: ss.280-290

Özet

A marked decrease in the saturation magnetization by the formation of functional shells around the magnetic core is an important disadvantage of magnetic core-shell nanoparticles. Another drawback of Ti(IV)-functionalized immobilized metal affinity chromatography (IMAC) sorbents is the acidic character of the binding medium used for Ti4+ attachment onto composite magnetic nanoparticles, which causes an additional decrease in the saturation magnetization owing to the chemical interaction between the acidic moiety and the magnetic core. An IMAC sorbent in the form of magnetic microspheres with superior and stable magnetic properties with respect to magnetic core-shell nanoparticles was designed for phosphopeptide enrichment. Magnetic, monodisperse-porous silica microspheres (MagSiO(2))(6) mu m in size were synthesized by a new staged-shape template hydrolysis-condensation protocol. A porous silica shell layer was generated around the microspheres to protect the magnetic core from the acidic medium during Ti4+ attachment (MagSiO(2)@SiO2). The MagSiO(2)@SiO2 microspheres were coated with a polydopamine shell (MagSiO(2)@SiO2@PDA) and Ti4+ was attached onto the composite microspheres (MagSiO(2)@SiO2@PDA@Ti(IV)). Formation of the PDA layer and Ti4+ attachment did not cause any significant decrease in the saturation magnetization. The platform exhibited excellent performance for phosphopeptide enrichment from the digests of phosphorylated proteins. Selectivity was investigated by matrix-assisted laser desorption/ionization time-of-flight mass spectrometry. The detection limit for phosphopeptide enrichment by the MagSiO(2)@SiO2@PDA@Ti(IV) microspheres from the tryptic digests of beta-casein was 50 fmol/mL. Usability of the proposed magnetic sorbent with complex biological samples was demonstrated by successful enrichment of four phosphopeptides from human serum. The proposed sorbent showed stable performance over five repeated uses. (C) 2017 Elsevier B.V. All rights