Photosensitized Effects of Rose Bengal on Structure and Function of Lens Protein (Articolo in rivista)

Type

• Articolo in rivista (Classe)
• Prodotto della ricerca (Classe)

Label

• Photosensitized Effects of Rose Bengal on Structure and Function of Lens Protein (Articolo in rivista) (literal)

Anno

• 2009-01-01T00:00:00+01:00 (literal)

Alternative label

• Youssef T, Kassem M, Abdella T, Harith MA, Lenci F. (2009)
  Photosensitized Effects of Rose Bengal on Structure and Function of Lens Protein
  in Photochemistry and photobiology
  (literal)

Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#autori

• Youssef T, Kassem M, Abdella T, Harith MA, Lenci F. (literal)

Pagina inizio

• 1306 (literal)

Pagina fine

• 1313 (literal)

Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#numeroVolume

• 85 (literal)

Rivista

• Photochemistry and photobiology (Rivista)

Note

• ISI Web of Science (WOS) (literal)

Titolo

• Photosensitized Effects of Rose Bengal on Structure and Function of Lens Protein (literal)

Abstract

• The conformational changes of the bovine lens protein \"alpha-crystallin\" have been investigated in the presence of the photosensitizer Rose Bengal (RB), in the dark as well as after visible light irradiation. Absorption and fluorescence emission spectra of RB [5 x 10(-6) M] and Fourier transform-IR spectra of alpha-crystallin [5 mg mL(-1)] were significantly altered upon RB alpha-crystallin complex formation. RB was found to bind to alpha-crystallin in a molecular pocket characterized by a low polarity, with Trp most likely involved in this interaction. The binding constant (K(b)) has been estimated to be of the order of 2.5 (mg/mL)(-1). The intrinsic fluorescence of alpha-crystallin was quenched through both dynamic and static mechanisms. Light-induced photosensitized effects showed structural modifications in alpha-crystallin, including tertiary and secondary structure (an increase in unordered structure) alterations. Notwithstanding those photoinduced structural variations detected in alpha-crystallin when complexed with RB, the protein still retains its ability to play the role of chaperone for beta-crystallin. (literal)

Prodotto di

• Istituto di biofisica (IBF) (Istituto)
• Processi Fotoindotti in Biomolecole e Cellule (MD.P01.003.001) (Modulo)

Autore CNR

• FRANCESCO LENCI (Unità di personale interno)

Incoming links:

Prodotto

• Istituto di biofisica (IBF) (Istituto)
• Processi Fotoindotti in Biomolecole e Cellule (MD.P01.003.001) (Modulo)

Autore CNR di

• FRANCESCO LENCI (Unità di personale interno)

Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#rivistaDi

• Photochemistry and photobiology (Rivista)