Aberration in the structural paradigm of lens protein α crystallin by UV-C irradiation View Full Text


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Article Info

DATE

2018-06

AUTHORS

R. K. Ghosh, T. Kar, B. Dutta, A. Pathak, R. Rakshit, R. Basak, A. Das, K. Waheeda, P. Basak, M. Bhattacharyya

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. More... »

PAGES

281-287

Identifiers

URI

http://scigraph.springernature.com/pub.10.1007/s13765-018-0351-y

DOI

http://dx.doi.org/10.1007/s13765-018-0351-y

DIMENSIONS

https://app.dimensions.ai/details/publication/pub.1101407960


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