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Trehalose Inhibits the Heat-Induced Formation of the Amyloid-Like Structure of Soluble Proteins Isolated from Human Cataract Lens

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Abstract

The age-dependent loss of solubility and aggregation of crystallins constitute the pathological hallmarks of cataract. Several biochemical and biophysical factors are responsible for the reduction of crystallins’ solubility and formation of irreversible protein aggregates, which display amyloid-like characteristics. The present study reports the heat-induced aggregation of soluble proteins isolated from human cataract lenses and the formation of amyloid-like structures. Exposure of protein at 55 °C for 4 h resulted in extensive (≈ 60%) protein aggregation. The heat-induced protein aggregates displayed substantial (≈ 20 nm) redshift in the wavelength of maximum absorption (λmax) of Congo red (CR) and increase in Thioflavin T (ThT) fluorescence emission intensity, indicating the presence of amyloid-like structures in the heat-induced protein aggregates. Subsequently, the addition of trehalose resulted in substantial inhibition of heat-induced aggregation and the formation of amyloid-like structure. The ability of trehalose to inhibit the heat-induced aggregation was found to be linearly dependent upon its concentration used. The optimum effect was observed in the presence of 30–40% (w/v) trehalose where the aggregated was found to be reduced from 60 to 30%. The present study demonstrated the ability to trehalose to inhibit the protein aggregation and interfere with the formation of amyloid-like structures.

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Acknowledgements

This work was supported by the research grant (Ref. No. EMR/2017/005417) sponsored by Science and Engineering Research Board (SERB), Department of Science and Technology (DST), Govt. of India, New Delhi, India. The authors express their sincere gratitude to Dr. Vivek Verma, Department of Biotechnology, Central University of Rajasthan and Dr. Manish Singh, Institute of Nano Science and Technology, Mohali, for their assistance in performing experiments in the manuscript.

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  1. Department of Biotechnology, Central University of Rajasthan, NH-8 Bandersindri, Kishangarh, Ajmer, Rajasthan, 305817, India

    Lakshman Ram, Chandrika Mittal & Jay Kant Yadav

  2. Department of Ophthalmology, Jawaharlal Nehru Medical College, Ajmer, Rajasthan, India

    Ram Swaroop Harsolia

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Ram, L., Mittal, C., Harsolia, R. et al. Trehalose Inhibits the Heat-Induced Formation of the Amyloid-Like Structure of Soluble Proteins Isolated from Human Cataract Lens. Protein J 39, 509–518 (2020). https://doi.org/10.1007/s10930-020-09919-8

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