Abstract
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.
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Acknowledgments
We are grateful to World Bank-ICZMP (54-ICZMP/3P), DST (FIST), UGC-CAS, UGC-UPE, and DBT-IPLS, Government of India for providing the instrumental facility in the Department of Biochemistry, Calcutta University. Turban Kar thanks to UGC-DAE Consortium for Scientific Research, New Delhi, India, for providing the financial assistance in the form of grants and fellowships.
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Ghosh, R.K., Kar, T., Dutta, B. et al. Aberration in the structural paradigm of lens protein α crystallin by UV-C irradiation. Appl Biol Chem 61, 281–287 (2018). https://doi.org/10.1007/s13765-018-0351-y
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DOI: https://doi.org/10.1007/s13765-018-0351-y