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首页> 外文期刊>Ukrainian Biochemical Journal >The fibrin Bβ125-135 site is involved in the lateral association of protofibrils
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The fibrin Bβ125-135 site is involved in the lateral association of protofibrils

机译：纤维蛋白Bβ125-135位点参与原生纤维的横向关联

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Earlier we reported that during the human fibrinogen to fibrin transition a neoantigenic determinant was exposed in the Bβ119-133 fragment, where a hinge locus is situated. The fibrin-specific mAb FnI-3c and its Fab-fragment with epitope in this fragment inhibited the lateral association of protofibrils. We suggested that the epitope coincided with a site involved in this process. In this work we investigated the epitope location more precisely and defined a functional role for its exposure in the hinge locus of the molecule. It was found that mAb FnI-3c bound to human, horse and rabbit fibrins, all of which have Lys in the position corresponding to human BβK130, but not to bovine and rat fibrins, which have other amino acid residues in this position, strongly suggesting that BβK130 provides the integral part of the epitope. This fact, homology data, and structural biological analysis of the amino acid sequences around BβK130 indicate that the site of interest is localized within Bβ125-135. The synthetic peptides Bβ121-138 and Bβ125-135, unlike their scrambled versions, bound to mAb FnI-3c in SPR analysis. Both peptides, but not their scrambled versions, inhibited the lateral association of protofibrils. The FnI-3c epitope is exposed after fibrinopeptide A cleavage and desA fibrin monomer formation. Structural biological analysis of the fibrinogen to fibrin transition showed a distinct increase of flexibility in the hinge locus. We propose that the structural transformation in the fibrin hinge regions leads to the conformation necessary for lateral association of protofibrils.
机译：我们之前的报道称，在人纤维蛋白原期间，纤维蛋白过渡，在Bβ119-133片段中暴露了新茴香肽的决定簇，其中铰链轨迹位于位于铰链基因座中。该片段中纤维蛋白特异性MAb FNI-3C及其具有表位的Fab片段抑制了原生纤维的侧向缔合。我们建议表现符合此过程中涉及的网站。在这项工作中，我们更精确地研究了表位位置，并确定了分子铰链轨迹暴露的功能作用。发现MAB FNI-3C与人，马和兔纤维林结合，所有这些都含有对应于人BβK130的位置，但不是牛和大鼠纤维素，其具有这种位置的其他氨基酸残基，强烈暗示BβK130提供表位的组成部分。 BβK130周围氨基酸序列的这种事实，同源性数据和结构生物学分析表明感兴趣的部位在Bβ125-135内局部化。合成肽Bβ121-138和Bβ125-135与其加扰版本不同，在SPR分析中结合MAb FNI-3C。两种肽，但不是它们的乱涂的版本，抑制了原纤维的横向缔合。在纤维蛋白肽裂解和DESA纤维蛋白单体形成之后暴露FNI-3C表位。纤维蛋白转变的纤维蛋白原的结构生物学分析显示出铰链基因座中的柔韧性的不同增加。我们提出纤维蛋白铰链区域的结构转化导致原子纤维侧侧缔合的构成。

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