Structural changes of methemoglobin after adsorption on bioactive glass, as a function of surface functionalization and salt concentration

被引:17
作者
Gruian, C. [1 ,2 ,3 ]
Vulpoi, A. [1 ,2 ]
Steinhoff, H. -J. [3 ]
Simon, S. [1 ,2 ]
机构
[1] Univ Babes Bolyai, Fac Phys, Cluj Napoca 400084, Romania
[2] Univ Babes Bolyai, Interdisciplinary Res Inst BioNanoSci, Cluj Napoca 400084, Romania
[3] Univ Osnabruck, Dept Phys, D-49069 Osnabruck, Germany
关键词
Electron paramagnetic resonance; Protein adsorption; Bioactive glasses; Salt concentration; SECONDARY STRUCTURE; PROTEIN ADSORPTION; T4; LYSOZYME; HEMOGLOBIN; BINDING; SITE; GLUTARALDEHYDE; ALBUMIN; TIRF; EPR;
D O I
10.1016/j.molstruc.2012.01.045
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
Functional protein adsorption at liquid solid interfaces has been intensively studied in the last years, however it is difficult to evidence directly conformational changes of the protein which are likely to appear upon adsorption. Spin labeling in combination with Electron Paramagnetic Resonance (EPR) spectroscopy was applied in this study to investigate adsorption of horse methemoglobin to bioactive glass (BC) similar in composition with 4555 Bioglass (R). X-band cw-EPR spectra of spin labeled methemoglobin in solution were compared to those obtained after adsorption on bioactive glass surface (functionalized and non-functionalized with glutaraldehyde), to extract information of the structure and dynamics in the vicinity of position beta-93. The concentration of methemoglobin adsorbed on BC substrate was determined from the intensity of cw-EPR spectra and correlated with images obtained by Scanning Electron Microscopy (SEM). Line shape analysis of the EPR spectra revealed that ionic strength does not induce significant conformational changes in the protein structure upon adsorption, however, the chemical treatment applied to the bioactive glass surface positively influences protein adsorption. (C) 2012 Elsevier B.V. All rights reserved.
引用
收藏
页码:20 / 26
页数:7
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