Spectral and thermal properties of novel eye lens ζ-crystallin

Spectral and thermal properties of novel eye lens ζ-crystallin

Eye lenses are exposed to thermal, solar radiations, dryness that enhances cataractogenesis. Some animal lenses contain novel proteins in bulk quantities. ζ-crystallin occurred in three ecologically divergent species, but it's physiological role not known. The truncated variant of ζ-crystallin...

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Bibliographic Details
Published in:International journal of biological macromolecules Vol. 102; pp. 1052 - 1058
Main Authors: Malik, Ajamaluddin, Albogami, Shurog, Alsenaidy, Abdulrahman M., Aldbass, Abeer M., Alsenaidy, Mohammad A., Khan, Shams Tabrez
Format: Journal Article
Language:English
Published: Netherlands Elsevier B.V 01-09-2017
Subjects:
Cataract
Dynamic multimode spectroscopy
Hydrogen-Ion Concentration
Lens, Crystalline - chemistry
Protein Stability
Protein Unfolding
Spectrum Analysis
Temperature
Thermal shift assay
zeta-Crystallins - chemistry
ζ-Crystallin
FPLC
Cataract
Amp
DTT
ζ-Crystallin
DMS
EDTA
L
rpm
CV
LB
IPTG
Imax
OD600
Tm
λmax
Ni-NTA
Thermal shift assay
Dynamic multimode spectroscopy
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Summary:Eye lenses are exposed to thermal, solar radiations, dryness that enhances cataractogenesis. Some animal lenses contain novel proteins in bulk quantities. ζ-crystallin occurred in three ecologically divergent species, but it's physiological role not known. The truncated variant of ζ-crystallin causes hereditary cataract. Guinea pig ζ-crystallin is temperature-sensitive and rapidly aggregates at 41°C. Camels adopted to survive above 50°C, which raises an interesting question about how it retains lens proteins in the soluble state? Here, we have optimized expression and purification of recombinant camel ζ-crystallin. We have studied thermodynamic and spectroscopic properties using orthogonal techniques. Dynamic multimode spectroscopy results showed that camel ζ-crystallin unfolds via single transition with Tm value of 60.8±0.1°C and van’t Hoff enthalpy of 714.7±7.1kJ/mol. Thermal-shift assay calculates Tm value of 62°C at pH 7. Additionally, the conformational stability of ζ-crystallin increases with ionic-strength. The influence of pH on ζ-crystallin was evaluated where the protein was found to be stable in the pH range of 6–9, but its stability drastically decreases below pH 6. Our results also showed that quaternary structure of ζ-crystallin drastically changed as a result of lowering pH. This study provides significant understandings onto the conformational, thermodynamic and unfolding pathway of camel ζ-crystallin.
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ISSN:0141-8130
1879-0003
DOI:10.1016/j.ijbiomac.2017.04.101