INFRARED SPECTROSCOPIC STUDIES OF TIME-DEPENDENT CHANGES IN FIBRINOGEN ADSORBED TO POLYURETHANES
INFRARED SPECTROSCOPIC STUDIES OF TIME-DEPENDENT CHANGES IN FIBRINOGEN ADSORBED TO POLYURETHANES
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DOI：
10.1021/la00056a030
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发表时间：
1991-08-01
期刊：
影响因子：
3.9
通讯作者：
CHITTUR, KK
中科院分区：
文献类型：
--
作者：
LENK, TJ;HORBETT, TA;CHITTUR, KK
通过使用衰减全反射红外流通池和测量通过暴露于 1% 十二烷基硫酸钠 (SDS) 溶液中可去除的蛋白质分数，研究了两种不同聚醚氨基甲酸酯脲上纤维蛋白原吸附层（约 300 ng/cm2）的时间依赖性转变。通过暴露于 SDS 去除的吸附纤维蛋白原的分数随着吸附蛋白质在表面上的停留时间而减少。红外光谱的变化与吸附的纤维蛋白原随时间的构象变化一致，特别是β结构（片状、转角和弯曲）的增加。还显示了吸附的纤维蛋白原的酰胺 II 带的重心频率偏移与 SDS 暴露后保留的纤维蛋白原量之间的相关性。两种类型的实验之间观察到的差异可以通过假设吸附蛋白质的结合态分布来解释。
Time-dependent transitions in an adsorbed layer of fibrinogen (approximately 300 ng/cm2) on two different poly(ether urethane ureas) were studied both by use of an attenuated total reflection infrared flow cell and by measurement of the fraction of protein removable by exposure to a 1% sodium dodecyl sulfate (SDS) solution. The fraction of the adsorbed fibrinogen removed by exposure to SDS decreased with residence time of the adsorbed protein on the surface. The infrared spectral changes are consistent with time-dependent conformational changes in the adsorbed fibrinogen, particularly a gain in beta-structures (sheets, turns, and bends). A correlation between the center-of-gravity frequency shift of the amide II band of adsorbed fibrinogen and the amount of fibrinogen retained after SDS exposure is also shown. Observed discrepancies between the two types of experiments can be explained by postulating a distribution of bound states for the adsorbed protein.