软X射线光谱显微镜探索贻贝粘附蛋白的介观形态学,Biomacromolecules

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软X射线光谱显微镜探索贻贝粘附蛋白的介观形态学
Biomacromolecules ( IF 5.5 ) Pub Date : 2021-02-18 , DOI: 10.1021/acs.biomac.0c01746
Yuji Higaki ₁ , Kazutaka Kamitani ₂ , Takuji Ohigashi ₃ , Teruaki Hayakawa ₄ , Atsushi Takahara _{2,

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Affiliation

海洋贻贝通过在脚尖腔中连续分泌贻贝脚蛋白来精确控制粘附斑的分层结构，从而在潮湿条件下有效地粘附。已经使用光谱显微镜对贻贝斑块的形态进行了化学分析。然而，由于常规化学成像技术的空间分辨率有限，介观形态尚未阐明。我们使用扫描透射软X射线光谱显微镜（STXM）研究了不均匀贻贝斑形态的化学形态。具有C 1s近边缘X射线吸收精细结构的高空间分辨率STXM化学成像可产生亚微米级不均匀贻贝斑形态的羟基取代芳族残基分布。基质由高蛋白密度的固化产物组成，其中包含大量的羟基取代的芳族碳，包括酪氨酸和3,4-二羟基苯丙氨酸（Dopa），而微区则是蛋白密度较差的区域，芳香族残基低相对含量。粘合剂界面被基质相覆盖以确保粘合。表皮层包含适度的多巴含量，这似乎已针对皮肤的机械性能进行了优化。

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Exploring the Mesoscopic Morphology in Mussel Adhesive Proteins by Soft X-ray Spectromicroscopy

Marine mussels efficiently adhere under wet conditions by precisely controlling the hierarchical structure of the adhesive plaque through sequential mussel foot protein secretion in the foot-tip cavity. Chemical analysis of the non-uniform mussel plaque morphology has been performed using spectromicroscopy; however, the mesoscopic morphology has not been elucidated yet because of the limited spatial resolution of conventional chemical imaging techniques. We investigated the chemical speciation in the non-uniform mussel plaque morphology employing scanning transmission soft X-ray spectromicroscopy (STXM). The high-spatial-resolution STXM chemical imaging with C 1s near-edge X-ray absorption fine structure yields the distribution of the hydroxy-substituted aromatic residues in the sub-micron scale non-uniform mussel plaque morphology. The matrix consists of a high-protein-density cured product containing a large number of hydroxy-substituted aromatic carbons, including tyrosine and 3,4-dihydroxyphenylalanine (Dopa), whereas the microdomains are poor-protein-density regions with a low aromatic residue relative content. The adhesive interface was covered with the matrix phase to ensure adhesion. The cuticle layer involves a moderate Dopa content, which appears to be optimized for the mechanical performance of the skin.

更新日期：2021-03-08

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