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Studies of the surface layer structure and properties of poly(styrene/α-t-butoxy-ω-polyglycidol) microspheres by carbon nuclear magnetic resonance,X-ray photoelectron spectroscopy,and the adsorption of human serum albumin and γ-globulins
Authors:Teresa Basinska  Stanislaw Slomkowski  Slawomir Kazmierski  Andrzej Dworak  Mohamed M Chehimi
Institution:1. Center of Molecular and Macromolecular Studies, Polish Academy of Sciences, Sienkiewicza 112, 90-363 Lodz, Poland;2. Institute of Coal Chemistry, Polish Academy of Sciences, Sowinskiego 5, 44-102 Gliwice, Poland;3. Institut de Topologie et de Dynamique des Systemes, Universite Paris 7, Denis Diderot, CNRS, 1 Rue Guy de la Brosse, 75005 Paris, France
Abstract:The composition and properties of the surface layers of poly(styrene/α-t-butoxy-ω-polyglycidol) poly(styrene/VB-polyGL)] microspheres synthesized by the radical copolymerization of styrene and α-t-butoxy-ω-vinylbenzyl-polyglycidol (VB-polyGL) macromonomers number-average molecular weight (Mn) = 950 or 2700] were investigated with X-ray photoelectron spectroscopy, 13C NMR, and the adsorption of human serum albumin and γ-globulins. The number-average diameter of the synthesized microspheres was 220 nm. Their surface layers were rich in polyglycidol, with polyglycidol-to-polystyrene unit ratios of 0.443 (VB-polyGL with Mn = 950) and 0.427 (VB-polyGL with Mn = 2700). In suspensions of poly(styrene/VB-polyGL) particles in D2O, the polymer chains in the polyglycidol-rich surface layers were highly mobile, allowing the registration of polyglycidol 13C NMR spectra with standard procedures for polymer solutions. In these spectra, the signals of the relatively immobile polystyrene segments were absent. The spin–lattice relaxation times (T1) measured for polyglycidol in the microsphere surface layers and for VB-polyGL macromonomers in solution were very close, indicating similar degrees of motion in bound (in particle surface layers) and free (in solution) polyglycidol macromolecules. Studies of protein adsorption revealed that hydrophilic polyglycidol layers were protein-repellent. It was found that longer polyglycidol chains in particle surface layers were more mobile (higher T1 values) and provided better protection against protein adsorption. © 2003 Wiley Periodicals, Inc. J Polym Sci Part A: Polym Chem 42: 615–623, 2004
Keywords:polymer microspheres  surface structure  NMR  XP5  human serum albumin  gamma globulins  protein adsorption
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