Effects of thermal denaturation and UV-B irradiation on eye lens crystallin proteins

M. Camilles, S. Link, A. Krushelnitsky, J. Balbach, K. Saalwächter

Institute of Physics, Martin Luther University Halle-Wittenberg, Germany

Crystallins are the major vision-related (i.e. refractive) proteins found in the eye lens. The mammalian lens consist of three classes of proteins, α-, β- and γ-crystallins, the former also acts as chaperone [1]. Commonly, proteins are subject to a continuous degradation and replacement process, but the eye lens proteins have no turnover and hence have to remain stable and soluble for a lifetime. So far, most studies have focused on single eye lens proteins and their interactions at low concentrations [2]. Here we combine NMR and other biophysical techniques to monitor stress induced aggregation and changes of the interactions of crystallins at various concentrations [3]. This allows us to investigate molecular effects which might lead to cataract in a highly concentrated eye lens surrounding.

[1] H. Bloemendal et. al., Progress in Biophysics & Molecular Biology 86 407-485 (2004). (link)
[2] CN Kingsley, R.W. Martin et.al., Structure 21, 2221 (2013). (link)
[3] M. Roos, S. Link et. al., Biophysical Journal 108, 98 (2015). (link)