Progression of Self-Assembly of Amelogenin Protein Supramolecular Structures in Simulated Enamel Fluid.

Progression of Self-Assembly of Amelogenin Protein Supramolecular Structures in Simulated Enamel Fluid.
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DOI:
10.1021/acs.biomac.8b00808
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发表时间:
2018-10-08
期刊:
影响因子:
6.2
通讯作者:
Habelitz S
Habelitz S
中科院分区:
化学2区
文献类型:
--
作者:
Engelberth SA;Bacino MS;Sandhu S;Li W;Bonde J;Habelitz S

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在牙釉质中,蛋白质引导的矿化机制,导致有序的纤维状磷灰石纳米晶体,仍然难以捉摸。体外研究表明,重组人釉原蛋白(RH174)是一种模板这一过程的基质蛋白,可以自组装成各种结构。本研究致力于阐明rH174在生理相关条件下的自组装。在模拟牙釉质液体中的自组装被监测长达2个月。在碱性(7.3-8.7)和酸性(5.5-6.1)的pH范围内,观察到从纳米球(17-23 nm)到中等长度的纳米棒的形成过程,最终形成了长的17-18 nm宽的带有纳米球的纳米带。在酸性条件下的组装进展更快,形成了具有较少持久纳米球的纳米带。X-射线衍射显示出反平行β片状反射的特征,支持淀粉样纳米带形成的模型。这是首次在碱性pH条件下观察到rH174纳米带以及同时形成纳米球,表明这两种超分子结构在生理条件下是稳定的。
Mechanisms of protein-guided mineralization in enamel, leading to organized fibrillar apatite nanocrystals, remain elusive. In vitro studies reveal recombinant human amelogenin (rH174), a matrix protein templating this process, self-assembles into a variety of structures. This study endeavors to clarify the self-assembly of rH174 in physiologically relevant conditions. Self-assembly in simulated enamel fluid was monitored up to 2 months. At alkali (7.3–8.7) and acidic (5.5–6.1) pH ranges, a distinct progression in formation was observed from nanospheres (17–23 nm) to intermediate-length nanorods, concluding with the formation of long 17–18 nm wide nanoribbons decorated with nanospheres. Assembly in acidic condition progressed quicker to nanoribbons with fewer persistent nanospheres. X-ray diffraction exhibited reflections characteristic of antiparallel β-sheets (4.7 and 9.65 Å), supporting the model of amyloid-like nanoribbon formation. This is the first observation of rH174 nanoribbons at alkaline pH as well as concurrent nanosphere formation, indicating both supramolecular structures are stable together under physiological conditions.
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