Investigation of mussel adhesive protein adsorption on polystyrene and poly(octadecyl methacrylate) using angle dependent XPS, ATR-FTIR, and AFM

被引:78
作者
Baty, AM
Suci, PA
Tyler, BJ
Geesey, GG
机构
[1] MONTANA STATE UNIV,CTR BIOFILM ENGN,BOZEMAN,MT 59717
[2] MONTANA STATE UNIV,DEPT MICROBIOL,BOZEMAN,MT 59717
[3] MONTANA STATE UNIV,DEPT CHEM ENGN,BOZEMAN,MT 59717
基金
美国国家科学基金会;
关键词
mussel adhesive protein; protein adsorption; XPS; ATR-FTIR; AFM;
D O I
10.1006/jcis.1996.0036
中图分类号
O64 [物理化学(理论化学)、化学物理学];
学科分类号
070304 ; 081704 ;
摘要
The irreversible adsorption of mussel adhesive proteins (MAP) from the marine mussel Mytilus edulis has been investigated on polystyrene (PS) and poly(octadecyl methacrylate) (POMA) surfaces using angle resolved X-ray photoelectron spectroscopy (XPS), attenuated total reflection Fourier transform infrared (ATR-FTIR) spectrometry, and atomic force microscopy (AFM), Angle resolved XPS was used to quantify the elemental composition with depth of the upper 90 Angstrom of the surface, and AFM was used to obtain the surface topography, The adsorption pattern of MAP, revealed by AFM images, is distinctly different on the two polymer surfaces and suggests that the substratum influences protein adhesion, The depth profiles of MAP, obtained from angle resolved XPS, show differences in nitrogen composition with depth for MAP adsorbed to PS and POMA, Infrared spectra of hydrated adsorbed MAP revealed significant differences in the amide III region and in two bands which may originate from residues in the tandemly repeated sequences of MAP, This data demonstrates that the chemistry of the polymer film that is present at the protein-polymer interface can influence protein-protein and protein-surface interactions. (C) 1996 Academic Press, Inc.
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页码:307 / 315
页数:9
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