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Thermal-induced Unfolding of β-Crystallin and Disassembly of its Oligomers Revealed by Temperature-Jump Time-Resolved Infrared Spectroscopy

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Chinese Journal of Chemical Physics 2013年第6期26卷 739-746,I0004页

作者： Shan-shan Li Ying-ying Yu De-yong Li Xiao-chuan He Yong-zhen Bao Yu-xiang Weng Laboratory of Soft Matter Physics Institute of Physics Chinese Academy of Sciences Beijing 100190China Beijing Key Laboratory of Diagnosis and Therapy of Retinal and Choroid Diseases Key Laboratory ofVision Loss and Restoration Ministry of Education Department of Ophthalmology Peking UniversityPeople's Hospital Belying 100044 China

β-Crystallins are the major structural proteins existing in the vertebrate lens, and their conformational stability is critical in maintaining the life-long transparency and refraction index of the lens. Seven subunits of β-crystallins naturally assemble into various heteroge- neous oligomers with different sizes. Here, we systematically investigated the thermal sta- bility of the different secondary structures present in β-Crystallins and then the dynamic process for the thermal-induced unfolding of β-crystallins by Fourier transform infrared spectroscopy-monitored thermal titration and temperature-jump nanosecond time-resolved IR difference absorbance spectra. Our results show that the N-terminal anti-parallel β-sheets in β-crystallin are the most unstable with a transition midpoint temperature at 36.0-2.1℃, leading to the formation of an intermediate consisting vastly of random coil structures. This intermediate structure is temporally assigned to that of the monomer generated by the thermal-induced disassembly of β-crystallin oligomers with a transition midpoint tempera- ture of 40.4-0.7℃. The global unfolding of β-crystallins that leads to denaturation and aggregation indicated by the formation of intermolecular anti-parallel β-sheets has a transi- tion midpoint temperature determined as 72.4-0.2 ℃. Temperature-jump time-resolved IR absorbance difference spectroscopy analysis further reveals that thermal-induced unfolding of β-crystallins occurs firstly in the anti-parallel β-sheets in the N-terminal domains with a time constant of 50 ns.

关键词： β-Crystallin protein dynamical structure Temperature-jump Time-resolved IR spectrum

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