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

Autor(en): Gruian, C.
Vulpoi, A.
Steinhoff, H. -J.
Simon, S.
Stichwörter: ALBUMIN; BINDING; Bioactive glasses; Chemistry; Chemistry, Physical; Electron paramagnetic resonance; EPR; GLUTARALDEHYDE; HEMOGLOBIN; PROTEIN ADSORPTION; Salt concentration; SECONDARY STRUCTURE; SITE; T4 LYSOZYME; TIRF
Erscheinungsdatum: 2012
Herausgeber: ELSEVIER
Volumen: 1015
Startseite: 20
Seitenende: 26
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.
ISSN: 00222860
DOI: 10.1016/j.molstruc.2012.01.045

Show full item record

Page view(s)

Last Week
Last month
checked on Feb 27, 2024

Google ScholarTM