Towards understanding of protein adsorption behavior on plasma polymerized pyrrole film

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• 作者：Zhihong Zhang (1) mainzhh@163.com
  Guijuan Li (1)
  Fufeng Yan (1)
  Xianjun Zheng (1)
  Xili Li (1)
• 关键词：Plasma polymerization – ; Bovine serum albumin – ; Protein adsorption – ; Surface plasmon resonance spectroscopy – ; Electrochemical impedance spectroscopy
• 刊名：Central European Journal of Chemistry
• 出版年：2012
• 出版时间：August 2012
• 年：2012
• 卷：10
• 期：4
• 页码：1157-1164
• 全文大小：912.8 KB
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• 作者单位：1. Henan Provincial Key Laboratory of Surface & Interface Science, Zhengzhou University of Light Industry, Zhengzhou, 450002 China
• 刊物类别：Chemistry and Materials Science
• 刊物主题：Chemistry
  Chemistry
  Biochemistry
  Biophysics and Biomedical Physics
  Geochemistry
  
• 出版者：Versita, co-published with Springer-Verlag GmbH
• ISSN：1644-3624

文摘

Plasma polymerized pyrrole-like (PPpy) films exhibit good environmental stability and offer high reactivity with biomolecules. The present paper follows on from previous work on PPpy films applied as DNA immobilization/hybridization and describes the adsorption kinetics of bovine serum albumin (BSA) on PPpy films. Atom force microscopy was used to detect the surface roughness of PPpy surfaces obtained at different input powers or for different polymerization time, including the surface roughness before and after BSA adsorption. The influence of experimental conditions (i.e., the plasma input power, the polymerization time, the concentration of BSA, and the pH values of buffer solutions) on protein adsorption was investigated in situ by Surface plasmon resonance spectroscopy (SPR). SPR analysis confirmed the differently dynamic adsorption behavior of BSA on PPpy films under various experimental conditions. The adsorption constant, K _a , was deduced from Langmuir isotherm equations, which were simulated using experimental data collected by SPR and electrochemical impedance spectroscopy (EIS). Analysis of the combination data of SPR and EIS indicates that PPpy films under various conditions show completely different adsorption behaviors and could be applied as biomaterials for electrochemical protein sensing or as protein-resistant.