Complexity of "A-a" knob-hole fibrin interaction revealed by atomic force spectroscopy
Complexity of "A-a" knob-hole fibrin interaction revealed by atomic force spectroscopy
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DOI：
10.1021/la703264x
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发表时间：
2008-05-06
期刊：
影响因子：
3.9
通讯作者：
Schoenfisch, Mark H.
中科院分区：
文献类型：
--
作者：
Averett, Laurel E.;Geer, Carri B.;Schoenfisch, Mark H.
在血管损伤期间，纤维蛋白原转化为纤维蛋白，纤维蛋白是一种用作血凝块结构支架的聚合物。纤维蛋白的主要功能是承受血液中的大剪切力，并为凝块提供机械稳定性，保护伤口。了解维持纤维蛋白结构所涉及的生物物理力是生物医学界的极大兴趣。以前的报道已经确定了“A-a”旋钮-孔相互作用作为负责纤维蛋白结构完整性的主导力。在本文中，生化力光谱用于研究纤维蛋白片段和变体纤维蛋白原分子之间的钮-孔相互作用，以识别个体纤维蛋白分子之间发生的力。“A-a”旋钮-孔相互作用的破裂导致先前在纤维蛋白力光谱中未报告的特征性曲线，具有两种不同的比力群体：110 +/- 34和224 +/- 31 pN。在没有功能性的“A”旋钮或孔“a”的情况下，这些力不再存在。我们建议，特征图案代表的D区纤维蛋白原的变形之前的“A-一个”钮孔键断裂。
During blood vessel injury, fibrinogen is converted to fibrin, a polymer that serves as the structural scaffold of a blood clot. The primary function of fibrin is to withstand the large shear forces in blood and provide mechanical stability to the clot, protecting the Wound. Understanding the biophysical forces involved in maintaining fibrin structure is of great interest to the biomedical community. Previous reports have identified the "A-a" knob-hole interaction as the dominant force responsible for fibrin's Structural integrity. Herein, biochemical force spectroscopy is used to study knob-hole interactions between fibrin fragments and variant fibrinogen molecules to identify the forces occurring between individual fibrin molecules. The rupture of the "A-a" knob-hole interaction results in a characteristic profile previously unreported in fibrin force spectroscopy with two distinct Populations of specific forces: 110 +/- 34 and 224 +/- 31 pN. In the absence of a functional "A" knob or hole "a", these forces cease to exist. We propose that the characteristic pattern represents the deformation of the D region of fibrinogen prior to the rupture of the "A-a" knob-hole bond.