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Aberration in the structural paradigm of lens protein α crystallin by UV-C irradiation
R. K. Ghosh,T. Kar,B. Dutta,A. Pathak,R. Rakshit,R. Basak,A. Das,K. Waheeda,P. Basak,M. Bhattacharyya 한국응용생명화학회 2018 Applied Biological Chemistry (Appl Biol Chem) Vol.61 No.3
The conformation of lens protein α crystallin was investigated using different spectroscopic techniques under normal and UV-C-irradiated condition. The structural elucidation of commercially available lens protein α crystallin under the effects of UV-C irradiation has never been reported earlier. To study the effects of irradiation on the lens protein, we used UV–visible spectroscopy, CD spectroscopy, and steady-state and time-resolved fluorescence measurements along with FTIR study, under increasing doses of UV-C irradiation. Using the secondary and tertiary structural changes as parameters for detecting conformational perturbation, we investigated the structural paradigm shift in the lens protein α crystallin. Increasing doses of UV-C radiation resulted in decreasing β sheet content of α crystallin from 30 to 10%. The fluorescence profile confirmed the formation of ROS species in the protein upon extensive exposure to UV-C irradiation. These results inferred UV-C irradiation may induce alteration of secondary structure of the lens protein leading to impaired biological functioning.
Aberration in the structural paradigm of lens protein α crystallin by UV-C irradiation
Ghosh, R.K.,Kar, T.,Dutta, B.,Pathak, A.,Rakshit, R.,Basak, R.,Das, A.,Waheeda, K.,Basak, P.,Bhattacharyya, M. The Korean Society for Applied Biological Chemistr 2018 Applied Biological Chemistry (Appl Biol Chem) Vol.61 No.3
The conformation of lens protein ${\alpha}$ crystallin was investigated using different spectroscopic techniques under normal and UV-C-irradiated condition. The structural elucidation of commercially available lens protein ${\alpha}$ crystallin under the effects of UV-C irradiation has never been reported earlier. To study the effects of irradiation on the lens protein, we used UV-visible spectroscopy, CD spectroscopy, and steady-state and time-resolved fluorescence measurements along with FTIR study, under increasing doses of UV-C irradiation. Using the secondary and tertiary structural changes as parameters for detecting conformational perturbation, we investigated the structural paradigm shift in the lens protein ${\alpha}$ crystallin. Increasing doses of UV-C radiation resulted in decreasing ${\beta}$ sheet content of ${\alpha}$ crystallin from 30 to 10%. The fluorescence profile confirmed the formation of ROS species in the protein upon extensive exposure to UV-C irradiation. These results inferred UV-C irradiation may induce alteration of secondary structure of the lens protein leading to impaired biological functioning.