Suppr超能文献

吸附后纤维蛋白原的构象变化

Conformational changes of fibrinogen after adsorption.

作者信息

Clarke Matthew L, Wang Jie, Chen Zhan

机构信息

Department of Chemistry, University of Michigan, Ann Arbor, Michigan 48109, USA.

出版信息

J Phys Chem B. 2005 Nov 24;109(46):22027-35. doi: 10.1021/jp054456k.

Abstract

The adsorption behavior of fibrinogen to two biomedical polyurethanes and a perfluorinated polymer has been investigated. Changes in the secondary structure of adsorbed fibrinogen were monitored using attenuated total reflection Fourier transform infrared spectroscopy (ATR-FTIR) and sum frequency generation vibrational spectroscopy (SFG). SFG measurements were performed in the amide I range as well as in the C-H/N-H stretching range. Amide I signals from SFG demonstrate that fibrinogen has post-adsorption conformational changes that are dependent upon the polymer surface properties. For example, strong attenuation of the amide I and N-H stretching signals with increasing residence time was observed for fibrinogen adsorbed to poly(ether urethane) but not for the other two polymers. This change is not readily observed by ATR-FTIR. Differences in the observed spectral changes for fibrinogen adsorbed to each polymer are explained by different initial binding mechanisms and post-adsorption conformational changes.

摘要

研究了纤维蛋白原在两种生物医学聚氨酯和一种全氟聚合物上的吸附行为。使用衰减全反射傅里叶变换红外光谱(ATR-FTIR)和和频振动光谱(SFG)监测吸附的纤维蛋白原二级结构的变化。SFG测量在酰胺I范围以及C-H/N-H伸缩范围进行。来自SFG的酰胺I信号表明,纤维蛋白原在吸附后发生构象变化,这取决于聚合物的表面性质。例如,观察到吸附在聚(醚聚氨酯)上的纤维蛋白原随着停留时间的增加,酰胺I和N-H伸缩信号强烈衰减,而其他两种聚合物则没有。这种变化在ATR-FTIR中不易观察到。吸附在每种聚合物上的纤维蛋白原所观察到的光谱变化差异,是由不同的初始结合机制和吸附后构象变化所解释的。

文献AI研究员

20分钟写一篇综述,助力文献阅读效率提升50倍。

立即体验

用中文搜PubMed

大模型驱动的PubMed中文搜索引擎

马上搜索

文档翻译

学术文献翻译模型,支持多种主流文档格式。

立即体验