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首页> 外文期刊>Crystal growth & design >Identification of an 'acidic' C-terminal mineral modification sequence from the mollusk shell protein Asprich
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Identification of an 'acidic' C-terminal mineral modification sequence from the mollusk shell protein Asprich

机译：从软体动物壳蛋白Asprich鉴定“酸性” C端矿物修饰序列

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摘要

The formation of the mineralized mollusk shell involves the participation specific proteins to control mineral formation and morphology. Recent sequencing studies have identified a subfamily of seven proteins that are specific for the prismatic or calcitic layer of the mollusk Atrina rigida. This subfamily, named Asprich a through a, are polyanionic in sequence and contain conserved sequence regions at the N- and C-termini that are believed to play a role in mineral formation. Using solid-phase peptide synthesis. we have recreated the 42-AA C-terminal domain of Asprich which contains two conserved subdomains, the 17 AA Asp, Glu, Ala repeat (DEAD 17) and the Asp. Glu-rich 25 AA acidic-2 region. Using in vitro calcium carbonate mineralization assays, we demonstrate that the 42 AA C-terminal domain exerts effects on the morphology of forming calcite crystals, leading to the formation of porosities and irregular crystal growth. The two subdomains, DEAD 17 and acidic-2, exert similar, albeit weaker. effects on crystal growth as well. Interestingly. when DEAD 17 and acidic-2 are present as free peptides in a 1: 1 mole mixture in parallel mineralization assays, the resulting peptide-mediated effects on calcite morphology are dramatically different from the results obtained for either the 42 AA C-terminal domain or the individual DEAD 17 and acidic-2 domains themselves. These results suggest that the functionality of the individual DEAD17 and acidic-2 subdomains can be transformed depending upon the presence of other free peptide species. Structurally, the 42 AA C-terminal domain and the two subdomains are remarkably similar to one another and are conformationally labile, existing in an equilibrium with random-coil and other undefined secondary structures at neutral pH, traits that are also common to calcium carbonate-specific polypeptide sequences.
机译：矿化的软体动物壳的形成涉及参与蛋白，以控制矿物质的形成和形态。最近的测序研究已经确定了七个蛋白质的亚科，这些蛋白质对软体动物Atrina hardica的棱柱或钙质层具有特异性。这个亚家族命名为Asprich a到a，在序列上是聚阴离子，并在N和C端含有保守的序列区域，据信这在矿物形成中起作用。采用固相肽合成法。我们已经重建了Asprich的42-AA C末端结构域，其中包含两个保守的亚结构域，分别是17个Aa Asp，Glu，Ala重复序列（DEAD 17）和Asp。富含Glu的25 AA酸性2区。使用体外碳酸钙矿化测定法，我们证明42 AA C末端域对方解石晶体形成的形态产生影响，导致形成孔隙和不规则晶体生长。两个子域，DEAD 17和酸性2，尽管作用较弱，但作用相似。对晶体生长的影响。有趣的是。在平行矿化测定中，当DEAD 17和酸性2作为游离肽以1：1摩尔的混合物形式存在时，所得的肽介导的方解石形态影响与42 AA C端结构域或各个DEAD 17和酸性2域本身。这些结果表明，取决于其他游离肽种类的存在，可以转化单个DEAD17和酸性2亚结构域的功能。在结构上，42个AA C末端结构域和两个亚结构域彼此非常相似，并且构象不稳定，在中性pH下与无规卷曲和其他不确定的二级结构平衡存在，这些特征也是碳酸钙所共有的。特异性多肽序列。

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