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首页> 外文期刊>Proceedings of the National Academy of Sciences of the United States of America >Direct observation of the anchoring process during the adsorption of fibrinogen on a solid surface by force-spectroscopy mode atomic force microscopy
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Direct observation of the anchoring process during the adsorption of fibrinogen on a solid surface by force-spectroscopy mode atomic force microscopy

机译：力谱模式原子力显微镜直接观察纤维蛋白原在固体表面吸附过程中的锚固过程

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摘要

Atomic force microscopy in a force- spectroscopy mode has been used to investigate the kinetics of the adsorption process of fibrinogen molecules on a silica surface. An original "approach/retraction" cycle of the tip/ surface was used for this purpose. Fibrinogen molecules were adsorbed on the atomic force microscopy tip and were brought into contact with the silica surface for different interaction times varying from 5 to 2,000 ms. Multiple consecutive ruptures were observed. The mean number of ruptures n_r per cycle increases steadily with the interaction time as well as the mean strength f_r which varies from 300 pN for 5 ms to 1,400 pN for 2,000 ms. The minimal interaction timc for a fibrinogen molecule to bind strongly to a silica surface during an adsorption process appears to lie between 50 and 200 ms. The histograms of the distances between two consecutive ruptures in one cycle exhibit maxima around 20-25 nm. This length is comparable to the characteristic distance between D and E globules of one fibrinogen molecule and suggests that fibrin- ogen molecules mainly adsorb through their D and E globules.
机译：力光谱模式的原子力显微镜已用于研究血纤蛋白原分子在二氧化硅表面上吸附过程的动力学。尖端/表面的原始“接近/回缩”循环用于此目的。纤维蛋白原分子吸附在原子力显微镜尖端上，并与二氧化硅表面接触，相互作用时间从5到2,000 ms不等。观察到多次连续破裂。每个周期的平均断裂数n_r随相互作用时间以及平均强度f_r稳步增加，从5 ms的300 pN到2,000 ms的1,400 pN不等。在吸附过程中，纤维蛋白原分子与二氧化硅表面牢固结合的最小相互作用时间似乎在50到200毫秒之间。一个周期中两次连续破裂之间的距离直方图在20-25 nm附近显示最大值。该长度可与一个纤维蛋白原分子的D和E小球之间的特征距离相媲美，这表明纤维蛋白原分子主要通过其D和E小球吸收。

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