Vibrational spectroscopic studies on fibrinogen adsorption at polystyrene/protein solution interfaces: Hydrophobic side chain and secondary structure changes
Vibrational spectroscopic studies on fibrinogen adsorption at polystyrene/protein solution interfaces: Hydrophobic side chain and secondary structure changes
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DOI：
10.1021/jp0534683
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发表时间：
2006-03-16
影响因子：
3.3
通讯作者：
Chen, Z
中科院分区：
文献类型：
--
作者：
Wang, J;Chen, XY;Chen, Z
采用和频振动光谱（SFG）和衰减全反射傅里叶变换红外光谱（ATR-FTIR）原位研究了纤维蛋白原吸附到聚苯乙烯（PS）/蛋白质溶液界面后的结构变化。吸附纤维蛋白原分子的疏水侧链和二级结构的不同行为已被观察到。我们的研究结果表明，吸附后，疏水性PS表面诱导纤维蛋白原分子的快速结构变化，通过调整纤维蛋白原中的一些疏水性侧链，使它们面对的表面。纤维蛋白原疏水侧链的这种结构变化是局部变化，不会立即引起蛋白质二级结构的显著变化。我们的研究还表明，吸附的纤维蛋白原和PS表面之间的相互作用可以诱导蛋白质的二级结构或全局构象发生显着的变化，在一个更长的时间尺度。
Structural changes of fibrinogen after adsorption to polystyrene (PS) were examined at the PS/protein solution interface in situ using sum frequency generation (SFG) vibrational spectroscopy and attenuated total reflection Fourier transform infrared spectroscopy (ATR-FTIR). Different behaviors of hydrophobic side chains and secondary structures of adsorbed fibrinogen molecules have been observed. Our results indicate that upon adsorption, the hydrophobic PS surface induces fast structural changes of fibrinogen molecules by aligning some hydrophobic side chains in fibrinogen so that they face to the surface. Such structural changes of fibrinogen hydrophobic side chains are local changes and do not immediately induce significant changes of the protein secondary structures. Our research also shows that the interactions between adsorbed fibrinogen and the PS surface can induce significant changes of protein secondary structures or global conformations which occur on a much longer time scale.