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 spectromic...
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Veröffentlicht in: | Biomacromolecules 2021-03, Vol.22 (3), p.1256-1260 |
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Sprache: | eng |
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Zusammenfassung: | 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. |
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ISSN: | 1525-7797 1526-4602 |
DOI: | 10.1021/acs.biomac.0c01746 |