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首頁> 外文學(xué)位 >Single-molecule force spectroscopy studies of fibrin 'A-a' polymerization interactions via the atomic force microscope.
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Single-molecule force spectroscopy studies of fibrin 'A-a' polymerization interactions via the atomic force microscope.

機譯：通過原子力顯微鏡對血纖蛋白“ A-a”聚合反應(yīng)的單分子力譜研究。

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摘要

Fibrin, the polymerized form of the soluble plasma protein fibrinogen, plays a critical role in hemostasis as the structural scaffold of blood clots. The primary functions of fibrin are to withstand the shear forces of blood flow and provide mechanical stability to the clot, protecting the wound. While studies have investigated the mechanical properties of fibrin constructs, the response to force of critical polymerization interactions such as the 'A--a' knob--hole interaction remains unclear. Herein, the response of the 'A--a' bond to force was examined at the single-molecule level using the atomic force microscope. Force spectroscopy methodology was developed to examine the 'A--a' interaction while reducing the incidence of both nonspecific and multiple molecule interactions. The rupture of this interaction resulted in a previously unreported characteristic force profile comprised of up to four events. We hypothesized that the first event represented reorientation of the fibrinogen molecule, the second and third represented unfolding of structures in the D region of fibrinogen, and the last event was the rupture of the 'A--a' bond weakened by prior structural unfolding. The configuration, molecular extension, and kinetic parameters of each event in the characteristic pattern were examined to compare the unfolding of fibrin to other proteins unfolded by force. Fitting the pattern with polymer models showed that the D region of fibrinogen could lengthen by ∼50% of the length of a fibrin monomer before rupture of the 'A--a' bond. Analysis showed that the second and third events had kinetic parameters similar to other protein structures unfolded by force. Studies of the dependence of the characteristic pattern on calcium, concentration of sodium chloride, pH, and temperature demonstrated that the incidence of the last event was affected by solution conditions. However, only low pH and high temperatures reduced the probability that an interaction was characteristic, indicating that the force required to rupture the 'A--a' bond was less sensitive than the bond's resilience to structural unfolding to solution conditions. The structural unfolding that precedes the rupture of the 'A--a' bond may prove significant in the polymerization and mechanical properties of fibrin.
機譯：纖維蛋白是可溶性血漿蛋白纖維蛋白原的聚合形式，在止血過程中起著血凝塊的結(jié)構(gòu)支架的作用。纖維蛋白的主要功能是承受血流的剪切力并為凝塊提供機械穩(wěn)定性，從而保護傷口。盡管研究已經(jīng)研究了纖維蛋白結(jié)構(gòu)的機械性能，但對于關(guān)鍵的聚合反應(yīng)（例如``A--a''旋鈕-孔相互作用）的作用力的響應(yīng)仍然不清楚。在此，使用原子力顯微鏡在單分子水平上檢查了“ A-a”鍵對力的響應(yīng)。力譜方法學(xué)被開發(fā)用于檢查'A-a'相互作用，同時減少非特異性和多分子相互作用的發(fā)生率。這種相互作用的破裂導(dǎo)致以前未報告的特征力曲線，其中包括多達(dá)四個事件。我們假設(shè)第一個事件代表纖維蛋白原分子的重新定向，第二個和第三個事件代表纖維蛋白原D區(qū)結(jié)構(gòu)的展開，最后一個事件是“ A-a”鍵的斷裂，該鍵被先前的結(jié)構(gòu)展開削弱了。檢查了特征模式中每個事件的構(gòu)型，分子延伸和動力學(xué)參數(shù)，以比較纖維蛋白與通過力展開的其他蛋白質(zhì)的展開。用聚合物模型擬合該圖表明，在“ A-a”鍵斷裂之前，纖維蛋白原的D區(qū)可以延長到纖維蛋白單體長度的50％左右。分析表明，第二和第三事件的動力學(xué)參數(shù)類似于用力展開的其他蛋白質(zhì)結(jié)構(gòu)。對特征模式對鈣，氯化鈉濃度，pH和溫度的依賴性的研究表明，最后事件的發(fā)生受溶液條件的影響。但是，只有低pH值和高溫才降低了相互作用具有特征性的可能性，這表明斷裂'A-a'鍵所需的作用力不如鍵對結(jié)構(gòu)在溶液條件下展開的彈性敏感。 ``A-a''鍵斷裂之前的結(jié)構(gòu)展開可能證明對血纖蛋白的聚合和機械性能具有重要意義。

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  • 作者

    Averett, Laurel E.;

  • 作者單位

    The University of North Carolina at Chapel Hill.;

  • 授予單位 The University of North Carolina at Chapel Hill.;
  • 學(xué)科 Physics General.;Biophysics General.
  • 學(xué)位 Ph.D.
  • 年度 2010
  • 頁碼 218 p.
  • 總頁數(shù) 218
  • 原文格式 PDF
  • 正文語種 eng
  • 中圖分類
  • 關(guān)鍵詞

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