Aberration in the structural paradigm of lens protein alpha crystallin by UV-C irradiation

作者：Ghosh R K; Kar T; Dutta B; Pathak A; Rakshit R; Basak R; Das A; Waheeda K; Basak P^*; Bhattacharyya M^*

来源：Applied Biological Chemistry, 2018, 61(3): 281-287.

DOI：10.1007/s13765-018-0351-y

• alpha Crystallin
• FTIR
• Fluorescence spectroscopy
• Secondary structure
• UV-C irradiation

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.

• 出版日期2018-6