ADSORPTION OF HORSE METHEMOGLOBIN ON BIOACTIVE GLASS AT HIGH SALT CONCENTRATION, STUDIED BY EPR AND FTIR SPECTROSCOPY
| Autor(en): | Gruian, Cristina Steinhoff, Heinz-Juergen Simon, Simion |
Stichwörter: | bioactive glasses; Chemistry; Chemistry, Multidisciplinary; CONFORMATION; FTIR spectroscopy; MONOLAYERS; MOTION; protein adsorption; PROTEIN SECONDARY STRUCTURE; SITE; site-directed spin labeling; SPECTRA; SURFACE FUNCTIONALIZATION; T4 LYSOZYME; TIRF; TRANSFORM INFRARED-SPECTROSCOPY | Erscheinungsdatum: | 2011 | Herausgeber: | UNIV BABES-BOLYAI | Journal: | STUDIA UNIVERSITATIS BABES-BOLYAI CHEMIA | Volumen: | 56 | Ausgabe: | 3 | Startseite: | 71 | Seitenende: | 81 | Zusammenfassung: | Although protein adsorption has been intensively studied in the last years, conformational changes which are likely to appear on the structure of the protein upon adsorption are difficult to evidence directly. Combined SDSL and EPR spectroscopy were applied to study adsorption of horse mehemoglobin methemoglobin on bioactive glass in solution with high salt concentration (500mM NaCl). Further studies using FTIR spectroscopy aimed at identifying changes in the secondary structure of the protein upon the adsorption process. EPR spectra of methemoglobin spin labeled at position beta-93 in solution were compared to those obtained after adsorption to extract structural information. A consistent analysis of EPR spectra revealed that the adsorption of methemoglobin is influenced by the chemical treatment applied to the surface of bioactive glass. From the FTIR spectra details concerning the changes of secondary structure of the protein after 2 hours of sample immersion in protein solution were obtained. |
ISSN: | 12247154 |
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