Silica condensation by a silicatein α homologue involves surface-induced transition to a stable structural intermediate forming a saturated monolayer.

Silica condensation by a silicatein α homologue involves surface-induced transition to a stable structural intermediate forming a saturated monolayer.
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硅酸盐α同系物的二氧化硅缩合涉及表面诱导转变为形成饱和单层的稳定结构中间体。

DOI:
10.1021/bm100932e
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发表时间:
2010
期刊:
影响因子:
6.2
通讯作者:
C. F. van der Walle
C. F. van der Walle
中科院分区:
化学2区
文献类型:
--
作者:
Siddharth V. Patwardhan;S. Holt;S. Kelly;M. Kreiner;C. Perry;C. F. van der Walle

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硅酸蛋白 α 存在于海生海绵 Tethya aurantium 的二氧化硅针的蛋白丝中,其结构主要为 β 片层。然而,它以可溶形式产生,具有类似于其组织蛋白酶 L 同系物的混合 α-螺旋/β-折叠结构。为了理解酶催化二氧化硅缩合中的这种构象转变,我们使用了一种功能性重组硅酸盐 α,称为 4SER。在溶液中,4SER 在 pH 7 时构象不稳定,很容易展开为可溶性 β-折叠中间体,失去大部分螺旋结构。这种 β-折叠中间体是在 4SER 从溶液中吸附到二氧化硅表面后出现的。 4SER 具有特别的表面活性,可在 SiO2 上从低本体浓度形成接近饱和的单层,而在高本体浓度时不会转变为多层。吸附的中间体在二氧化硅冷凝和干燥过程中保持稳定。我们认为海洋海绵骨针中硅酸盐α的β-折叠结构代表了一种稳定的结构中间体,是在吸附到二氧化硅表面后形成的。
Silicatein α exists within the protein filament of silica spicules of the marine sponge Tethya aurantium in a predominantly β-sheet structure. However, it is produced in a soluble form with mixed α-helix/β-sheet structure akin to its cathepsin L homologue. To understand this conformational transition in the context of enzyme catalyzed silica condensation, we used a functional, recombinant silicatein α termed 4SER. In solution, 4SER becomes conformationally unstable at pH 7 and readily unfolds to a soluble β-sheet intermediate, losing the majority of its helical structure. This β-sheet intermediate is present following adsorption of 4SER to a silica surface from solution. 4SER is particularly surface active, forming a near saturated monolayer on SiO2 from low bulk concentrations, without transition to multilayers at high bulk concentrations. The adsorbed intermediate remains stable during silica condensation and drying. We propose that the β-sheet structure for silicatein α in marine sponge spicules represents a stable structural intermediate, formed upon adsorption to the silica surface.
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