In this study we investigated the structural features of azurin, a blue copper-containing enzyme, upon encapsulation in tetramethoxysilane derived sol-gel glasses. Fluorescence spectroscopy revealed that gelation of inorganic networks does not affect the protein tertiary structure and only after two months solvent phase loss altered protein stability. In case of organically modified sol-gel matrices, the protein stability was reduced after encapsulation into hosts modified by adding 3-Mercaptopropyl-trimethoxysilane, 3-Glycidyloxypropyl-trimethoxysilane and Trimethoxy octylsilane, while it was found to be enhanced in networks doped with 3-Trimethoxysilyl-propyl methacrylate and 3-Aminopropyl-trimethoxysilane. In order to better investigate the effects of silica glasses on azurin stability, unfolding experiments of the protein, in solution or entrapped, were also performed in the presence of both methanol and guanidinium hydrochloride (GdHCl). Our results suggest that the matrix protects azurin against the aggregation induced by alcohol, and that the free energy change value upon unfolding by GdHCl was lower than the value calculated for azurin in solution and was dependent on the surface chemistry of silica matrix.

Bottini, M., DI VENERE, A., Tautz, L., Desideri, A., Lugli, P., Avigliano, L., et al. (2004). Structural Stability of Azurin Encapsulated in Sol-Gel Glasses: A Fluorometric Study. JOURNAL OF SOL-GEL SCIENCE AND TECHNOLOGY, 30(3), 205-214 [10.1023/B:JSST.0000039527.88843.18].

Structural Stability of Azurin Encapsulated in Sol-Gel Glasses: A Fluorometric Study

BOTTINI, MASSIMO;DI VENERE, ALMERINDA;DESIDERI, ALESSANDRO;LUGLI, PAOLO;AVIGLIANO, LUCIANA;ROSATO, NICOLA
2004-01-01

Abstract

In this study we investigated the structural features of azurin, a blue copper-containing enzyme, upon encapsulation in tetramethoxysilane derived sol-gel glasses. Fluorescence spectroscopy revealed that gelation of inorganic networks does not affect the protein tertiary structure and only after two months solvent phase loss altered protein stability. In case of organically modified sol-gel matrices, the protein stability was reduced after encapsulation into hosts modified by adding 3-Mercaptopropyl-trimethoxysilane, 3-Glycidyloxypropyl-trimethoxysilane and Trimethoxy octylsilane, while it was found to be enhanced in networks doped with 3-Trimethoxysilyl-propyl methacrylate and 3-Aminopropyl-trimethoxysilane. In order to better investigate the effects of silica glasses on azurin stability, unfolding experiments of the protein, in solution or entrapped, were also performed in the presence of both methanol and guanidinium hydrochloride (GdHCl). Our results suggest that the matrix protects azurin against the aggregation induced by alcohol, and that the free energy change value upon unfolding by GdHCl was lower than the value calculated for azurin in solution and was dependent on the surface chemistry of silica matrix.
2004
Pubblicato
Rilevanza internazionale
Articolo
Sì, ma tipo non specificato
Settore BIO/10 - BIOCHIMICA
English
Con Impact Factor ISI
Bottini, M., DI VENERE, A., Tautz, L., Desideri, A., Lugli, P., Avigliano, L., et al. (2004). Structural Stability of Azurin Encapsulated in Sol-Gel Glasses: A Fluorometric Study. JOURNAL OF SOL-GEL SCIENCE AND TECHNOLOGY, 30(3), 205-214 [10.1023/B:JSST.0000039527.88843.18].
Bottini, M; DI VENERE, A; Tautz, L; Desideri, A; Lugli, P; Avigliano, L; Rosato, N
Articolo su rivista
File in questo prodotto:
Non ci sono file associati a questo prodotto.

I documenti in IRIS sono protetti da copyright e tutti i diritti sono riservati, salvo diversa indicazione.

Utilizza questo identificativo per citare o creare un link a questo documento: https://hdl.handle.net/2108/26648
Citazioni
  • ???jsp.display-item.citation.pmc??? ND
  • Scopus 3
  • ???jsp.display-item.citation.isi??? 5
social impact