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首页> 外文期刊>Journal of Molecular Biology >Changes in the molecular packing of fibrillin microfibrils during extension indicate intrafibrillar and interfibrillar reorganization in elastic response.
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Changes in the molecular packing of fibrillin microfibrils during extension indicate intrafibrillar and interfibrillar reorganization in elastic response.

机译：延伸过程中原纤维蛋白微纤维分子堆积的变化表明弹性反应中的原纤维内和原纤维间重组。

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Fibrillin-rich microfibrils are the major structural components of the extracellular matrix that provide elasticity in a majority of connective tissues. The basis of elastic properties lies in the organization of fibrillin molecules, which, unfortunately, is still poorly understood. An X-ray diffraction study of hydrated fibrillin-rich microfibrils from zonular filaments has been conducted to give an insight into the molecular structure of microfibrils in intact tissue. A series of measurements was taken during controlled tissue extension to observe alterations in the lateral packing of microfibrils. Computer-generated simulated patterns were used to fit the experimental X-ray scattering data and to obtain the fibril diameter and lateral distance between the fibrils. The results suggest a nonlinear correlation between external strain and decrease in fibril diameter and lateral spacing. This was accompanied by a nonlinear increase in axial periodicity and a structure with a 160-nm periodicity, which is reported here for the first time using X-ray diffraction. These changes may reflect the unraveling of fibrillin from the complex folded arrangement into a linear structure. This finding supports a pleating model where fibrillin molecules are highly folded within the microfibrils; more importantly, the connection is made between the interaction of individual microfibrils and the change in their suprafibrillar coherent organization during extension. We suggest that the intermediate states observed in our study reflect sequential unfolding of fibrillin and can explain the process of its reversible unraveling.
机译：富含原纤维蛋白的微纤维是细胞外基质的主要结构成分，可在大多数结缔组织中提供弹性。弹性性质的基础在于原纤维蛋白分子的组织，不幸的是，人们对它的了解仍然很少。进行了X射线衍射研究了来自细丝的水合富含原纤维的微纤维，以深入了解完整组织中微纤维的分子结构。在受控的组织伸展过程中进行了一系列测量，以观察微纤维的侧向堆积的变化。计算机生成的模拟图案用于拟合实验X射线散射数据，并获得原纤维直径和原纤维之间的横向距离。结果表明外部应变与原纤维直径和横向间距的减小之间存在非线性关系。这伴随着轴向周期性的非线性增加和具有160nm周期性的结构，这是首次使用X射线衍射进行报道。这些变化可能反映了原纤维蛋白从复杂的折叠结构中解散为线性结构。这一发现支持了一种褶皱模型，其中原纤维蛋白分子在微原纤维中高度折叠。更重要的是，在延伸过程中，各个微纤维之间的相互作用与其上胫旁相干组织的变化之间建立了联系。我们建议在我们的研究中观察到的中间状态反映了原纤维蛋白的顺序展开，并可以解释其可逆展开的过程。

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