4.7 Article

Facile preparation of superparamagnetic surface-imprinted microspheres using amino acid as template for specific capture of thymopentin

Journal

APPLIED SURFACE SCIENCE
Volume 357, Issue -, Pages 1490-1498

Publisher

ELSEVIER SCIENCE BV
DOI: 10.1016/j.apsusc.2015.10.042

Keywords

Surface imprinting; Fragment imprinting; Amino acid; Thymopentin; Magnetic microspheres

Funding

  1. National Natural Science Foundation of China [21174111, 51433008]
  2. Graduate Starting Seed Fund of Northwestern Polytechnical University [Z2015157]

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Novel superparamagnetic surface-imprinted microspheres (SIMs) with molecularly imprinted shell layer were controllably synthesized via fragment imprinting and surface imprinting technique. The SIMs-Arg and SIMs-Lys microspheres were prepared by using L-arginine (L-Arg) and L-lysine (L-Lys) as pseudo-template molecule for specific rebinding to thymopentin (TP5), respectively. The characterization results revealed that both SIMs-Arg and SIMs-Lys were successfully prepared and possessed a high magnetic sensitivity. The rebinding-isotherm analyses of SIMs-Arg and SIMs-Lys showed that the Langmuir isotherm model was well fitted to the equilibrium data, indicating that only one kind of rebinding site was present in SIMs-Arg and SIMs-Lys. Besides, the kinetic properties of SIMs-Arg and SIMs-Lys both were well described by the pseudo-second-order kinetics model, which indicated that a chemical process may be the rate-limiting step in the rebinding process. Moreover, the magnetic imprinted microspheres were found to have a higher specificity for TP5 than that for immunostimulating peptide human (IPH). What is more, SIMs-Arg and SIMs-Lys were successfully applied for TP5 determination in urine. According to the maximum adsorption capacity, the imprinting factor and real sample experiment, it was noted that SIMs-Arg had better specific adsorption property for TP5 than SIMs-Lys. (C) 2015 Elsevier B.V. All rights reserved.

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