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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
Published in Springer Netherlands
2018
Volume: 61
   
Issue: 3
Pages: 281 - 287
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. © 2018, The Korean Society for Applied Biological Chemistry.
About the journal
JournalData powered by TypesetApplied Biological Chemistry
PublisherData powered by TypesetSpringer Netherlands
ISSN2468-0834
Open AccessYes