Marine mussel adhesion: biochemistry, mechanisms, and biomimetics

Marine mussel adhesion: biochemistry, mechanisms, and biomimetics
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DOI:
10.1080/01694243.2012.697703
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发表时间:
2013-10-01
影响因子:
2.3
通讯作者:
Wu, Jianping
Wu, Jianping
中科院分区:
材料科学3区
文献类型:
--
作者:
Bandara, Nandika;Zeng, Hongbo;Wu, Jianping

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紫贻贝(Mytilus Edulis)是一种固着生物,它具有独特的能力,可以利用其固定结构附着在各种有机和无机海洋表面上。对于贻贝的生存、移动和自卫来说,强烈的表面粘附力是必不可少的。贻贝丝状物中的贻贝蛋白是将软体贻贝组织通过末端的粘附斑连接到海洋表面的结构成分,而粘附性蛋白则负责贻贝的粘附性。粘附性蛋白质是含有高比例翻译后修饰氨基酸的小分子,如3,4-二羟基苯丙氨酸(DOPA)。高DOPA含量、小分子尺寸、蛋白质灵活性、金属离子的存在以及高度的氧化态使贻贝与表面有很强的粘附性。贻贝的黏附机制取决于贻贝蛋白质的组成和相互作用,以及它们与环境的相互作用。贻贝黏附蛋白的提取困难阻碍了其机理研究和实际应用。重组贻贝蛋白和仿生学的发展将促进我们对黏附机制的理解。本文综述了贻贝黏附蛋白的特性、黏附机制、黏附应用以及仿生生物聚合物的研究进展。
Common blue mussel (Mytilus edulis) is a sessile organism that has unique ability to attach to a wide array of organic and inorganic marine surfaces using its holdfast structures. Strong adhesion to surfaces is essential for mussel survival, movement, and self-defense. Mussel proteins from byssal thread are structural components connecting soft mussel tissues to marine surfaces via an adhesive plaque in the distal end, while adhesive proteins from byssal plaque are responsible for mussel adhesion. Adhesive proteins are small molecules containing a high proportion of post-translationally modified amino acids such as 3,4-dihydroxyphenylalanine (DOPA). High DOPA content, small molecular size, protein flexibility, the presence of metal ions, and a high oxidation state enable strong mussel adhesion to surfaces. Mussel adhesion mechanisms depend on the composition and interactions of mussel proteins, as well as their interactions with the environment. Difficulties in the extraction of mussel adhesion proteins hamper mechanism studies and their practical applications. Development of recombinant mussel proteins and biomimetics will advance our understanding of adhesion mechanisms. In this paper, recent advances in the characterization of mussel adhesive proteins (MAPs), mussel adhesion mechanisms, application of MAPs, and the development of biomimetic biopolymers are reviewed.