INEB
INEB
TitleSelf-assembly and surface structure of an amphiphilic graft copolymer, polystyrene-graft-ω-stearyl-poly(ethylene oxide)
Publication TypeJournal Article
2000
AuthorsJi, J, Feng, L, Qiu, Y, Yu, X, Barbosa, MA
JournalJournal of Colloid and Interface ScienceJ. Colloid Interface Sci.
Volume224
Issue2
Pagination255 - 260
Date Published2000///
00219797 (ISSN)
Amphiphilic copolymer, article, biomaterial, copolymer, crystal, differential scanning calorimetry, electron microscopy, electron spin resonance, hydrophobicity, macrogol, polystyrene, priority journal, protein assembly, protein binding, protein structure, Self-assembly, stearic acid, Surface structure, X ray analysis
Surface properties of the polystyrene-graft-ω-stearyl-poly(ethylene oxide) (PS-g-SPEO) have been characterized by X-ray photoelectron spectroscopy (XPS), differential scanning calorimetry (DSC), contact angle, and spin probe techniques. The XPS results indicate that the surface and bulk composition of the PS-g-SPEO copolymers differ remarkably from each other. The stearyl and EO components enrich at the copolymer/air interfaces due to the self-assembly of the stearyl groups. At the PS-g-SPEO-72.6 surface (the x in PS-g-SPEO-x indicates the bulk density of the SPEO in wt%), the self- assembly of the hydrophobic stearyl groups is strong enough to form a stable liquid crystalline phase as indicated by DSC. At polymer/water interfaces, PS-g-SPEO-72.6 presents a hydrophilic surface with low PEO mobility, whereas PS-g-SPEO-50.6 and PS-g-SPEO-31.0 present the hydrophobic surface with high PEO mobility. The two different types of the surfaces, with different characters in surface energy, surface mobility of PEO, and surface architecture of SPEO, will be quite valuable as models for detecting the synergistic action of the PEO chains and the stearyl groups (specific ligand for albumin binding) in protein solutions. (C) 2000 Academic Press.
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