Adhesion a la Moule
Adhesion a la Moule
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DOI：
10.1093/icb/42.6.1172
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发表时间：
2002-12-01
影响因子：
2.6
通讯作者：
Waite, JH
中科院分区：
文献类型：
--
作者：
Waite, JH
贻贝在湍流的潮间带中的固着生活方式归功于永久附着过程和生物化学的适应性调整。这些可以理解的吸引了科学的兴趣，因为这种附着是快速的，多功能的，坚韧的，并且不会被水的存在破坏。贻贝足丝的粘附垫含有至少六种不同的蛋白质，它们都具有独特的氨基酸3，4-二羟基苯丙氨酸（DOPA），浓度范围为0.1 - 30 mol %。斑块中蛋白质分布的研究表明，具有最高水平的DOPA的蛋白质，如mefp-3（20摩尔%）和mefp-5（30摩尔%），似乎在斑块和基质之间的界面处或附近占主导地位。虽然蛋白质中多巴的存在传统上与通过螯合物介导的或共价偶联的交联有关，但最近用天然和合成的含多巴多肽进行的实验表明，交联形成不是多巴的唯一命运。完整的多巴，特别是界面附近，可能是必要的极性表面的良好的化学吸附。均匀高的DOPA氧化成交联导致界面失效，但具有高的内聚强度，而低的DOPA氧化导致以内聚为代价的更好的粘附。确定平衡这两个极端所涉及的适应性对于理解海洋附着力至关重要。
Mussels owe their sessile way of life in the turbulent intertidal zone to adaptive adjustments in the process and biochemistry of permanent attachment. These have understandably attracted scientific interest given that the attachment is rapid, versatile, tough and not subverted by the presence of water. The adhesive pads of mussel byssus contain at least six different proteins all of which possess the peculiar amino acid 3, 4-dihydroxyphenylalanine (DOPA) at concentrations ranging from 0.1 to 30 mol %. Studies of protein distribution in the plaque indicate that proteins with the highest levels of DOPA, such as mefp-3 (20 mol %) and mefp-5 (30 mol %), appear to predominate at or near the interface between the plaque and substratum. Although the presence of DOPA in proteins has traditionally been associated with cross-linking via chelate-mediated or covalent coupling, recent experiments with natural and synthetic DOPA-containing polypeptides suggest that cross-link formation is not the only fate for DOPA. Intact DOPA, particularly near the interface, may be essential for good chemisorption to polar surfaces. Uniformly high DOPA oxidation to cross-links leads to interfacial failure but high cohesive strength, while low DOPA oxidation results in better adhesion at the expense of cohesion. Defining the adaptations involved in balancing these two extremes is crucial to understanding marine adhesion.