Reverse engineering of bioadhesion in marine mussels
Reverse engineering of bioadhesion in marine mussels
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DOI：
10.1111/j.1749-6632.1999.tb08513.x
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发表时间：
1999-01-01
期刊：
影响因子：
--
通讯作者：
Waite, JH
中科院分区：
文献类型：
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作者：
Waite, JH
海洋贻贝（Mytilus）是在潮湿、盐水和湍流环境中与各种固体表面结合的专家。结合是快速的、永久的、多用途的和以蛋白质为基础的。对于贻贝来说，粘接的形式是一根足丝——一束体外的线——每根线的一端与动物的活体组织相连，另一端由粘接的斑块固定。我们研究了基底斑块和线的组成和形成，希望在化学和材料科学中发现技术相关的创新。迄今为止从足跖骨中分离出的所有蛋白质都含有不寻常的氨基酸3,4-二羟基苯丙氨酸。这种残留物似乎具有双重功能，对吸附和内聚具有重要影响。一方面，它形成了各种较弱的分子相互作用，如金属螯合物、氢键和pi-阳离子：这些似乎在表面行为（吸附）中占主导地位。另一方面，3,4-二羟基苯基丙氨酸及其氧化还原偶联多巴醌可以介导基底蛋白之间共价交联的形成（内聚）。其中一个挑战，在制造功能仿生版本的物理粘附是了解这两种反应是如何平衡的。
Marine mussels (Mytilus) are experts at bonding to a variety of solid surfaces in a wet, saline and turbulent environment. Bonding is rapid, permanent, versatile and protein-based. Zn mussels, adhesive bonding takes the form of a byssus-a bundle of extracorporeal threads-each connected to Living tissues of the animal at one end and secured by an adhesive plaque at the other. We have investigated the composition and formation of byssal plaques and threads with the hope of discovering technologically relevant innovations in chemistry and materials science. All proteins isolated from the byssus to date share the quality of containing the unusual amino acid, 3,4-dihydroxyphenylalanine. This residue appears to have a dual functionality with significant consequences for adsorption and cohesion. On the one hand, it forms a diverse array of weaker molecular interactions such as metal chelates, H-bonds, and pi-cations: these appear to dominate in surface behavior (adsorption). On the other hand, 3,4-dihydroxyphenylelanine and its redox couple, dopaquinone, can mediate formation of covalent cross-links among byssal proteins (cohesion). One of the challenges in making functional biomimetic versions of byssal adhesion is to understand how these two reactivities are balanced.