Istituto di Biofisica     
Youssef T., Kassem M., Abdella T., Harith M. A., Lenci F. Photosensitized Effects of Rose Bengal on Structure and Function of Lens Protein "Alpha-Crystallin". In: Photochemistry and Photobiology, vol. 85 (6) pp. 1306 - 1313. Wiley, 2009.
The conformational changes of the bovine lens protein "α-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 10−6 m] and Fourier transform-IR spectra of α-crystallin [5 mg mL−1] were significantly altered upon RB α-crystallin complex formation. RB was found to bind to α-crystallin in a molecular pocket characterized by a low polarity, with Trp most likely involved in this interaction. The binding constant (Kb) has been estimated to be of the order of 2.5 (mg/mL)−1. The intrinsic fluorescence of α-crystallin was quenched through both dynamic and static mechanisms. Light-induced photosensitized effects showed structural modifications in α-crystallin, including tertiary and secondary structure (an increase in unordered structure) alterations. Notwithstanding those photoinduced structural variations detected in α-crystallin when complexed with RB, the protein still retains its ability to play the role of chaperone for β-crystallin.
URL: http://www3.interscience.wiley.com/journal/122578311/abstract
DOI: 10.1111/j.1751-1097.2009.00613.x
Subject α-crystallin
Rose Bengal

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