Adaptive synergy between catechol and lysine promotes wet adhesion by surface salt displacement
Adaptive synergy between catechol and lysine promotes wet adhesion by surface salt displacement
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DOI：
10.1126/science.aab0556
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发表时间：
2015-08-07
期刊：
影响因子：
56.9
通讯作者：
Butler, Alison
中科院分区：
文献类型：
--
作者：
Maier, Greg P.;Rapp, Michael V.;Butler, Alison
在生理流体和海水中，合成聚合物对固体表面的粘附受到高盐、pH值和水合作用的严重限制，但这些条件并没有阻止贻贝有效粘附的演变。贻贝足蛋白提供了关于粘附适应的见解：值得注意的是，儿茶酚多巴（3，4-二羟基苯丙氨酸）和赖氨酸残基的丰度和接近暗示了粘附中的协同相互作用。某些铁载体-细菌铁螯合剂-由成对的儿茶酚和赖氨酸功能组成，从而提供了一个方便的实验平台来探索生物粘附中的分子协同作用。这些铁载体和合成类似物在pH 3.5至7.5的盐水中对云母表现出稳健的粘附能（E-ad >= -15毫焦耳/平方米）并抗氧化。相邻的儿茶酚-赖氨酸位置提供了“一对二的冲击”，由此赖氨酸从矿物表面驱逐水合阳离子，允许儿茶酚结合到下面的氧化物。
In physiological fluids and seawater, adhesion of synthetic polymers to solid surfaces is severely limited by high salt, pH, and hydration, yet these conditions have not deterred the evolution of effective adhesion by mussels. Mussel foot proteins provide insights about adhesive adaptations: Notably, the abundance and proximity of catecholic Dopa (3,4-dihydroxyphenylalanine) and lysine residues hint at a synergistic interplay in adhesion. Certain siderophores-bacterial iron chelators-consist of paired catechol and lysine functionalities, thereby providing a convenient experimental platform to explore molecular synergies in bioadhesion. These siderophores and synthetic analogs exhibit robust adhesion energies (E-ad >= -15 millijoules per square meter) to mica in saline pH 3.5 to 7.5 and resist oxidation. The adjacent catechol-lysine placement provides a "one-two punch," whereby lysine evicts hydrated cations from the mineral surface, allowing catechol binding to underlying oxides.