Adhesion of mussel foot protein Mefp-5 to mica: an underwater superglue.

Adhesion of mussel foot protein Mefp-5 to mica: an underwater superglue.
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DOI:
10.1021/bi3002538
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发表时间:
2012-08-21
期刊:
影响因子:
2.9
通讯作者:
Waite JH
Waite JH
中科院分区:
生物学3区
文献类型:
--
作者:
Danner EW;Kan Y;Hammer MU;Israelachvili JN;Waite JH

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贻贝具有非凡的能力,可以将其固着物或足丝附着在各种潮湿、含盐、腐蚀和/或被生物膜污染的基质上。贻贝足蛋白-5 (Mefp-5) 是贻贝足丝粘附斑中的几种蛋白质之一。 3,4 二羟基苯丙氨酸 (Dopa) (~30 mol%) 的高含量及其位于斑块-基底界面附近的位置常常促使人们猜测 Mefp-5 在粘附中起着关键作用。使用表面力装置,我们表明在云母表面 Mefp-5 实现了接近 Ead = ~− 14 mJ/m2 的粘附能。这超过了另一种界面蛋白 Mefp-3 的粘附能 4-5 倍,并且大于生物素和链霉亲和素的高度定向单层之间的粘附力。云母的粘附力因其对多巴的依赖性而引人注目,多巴在还原条件和酸性 pH 条件下最稳定。 Mefp-5 与其自身以及与来自美味贻贝的 Mefp-3 也表现出强烈的蛋白质-蛋白质相互作用。
Mussels have a remarkable ability to attach their holdfast, or byssus, opportunistically to a variety of substrata that are wet, saline, corroded, and/or fouled by biofilms. Mytilus edulis foot protein-5 (Mefp-5) is one of several proteins in the byssal adhesive plaque of the mussel M. edulis. The high content of 3,4 dihydroxyphenylalanine (Dopa) (~30 mol%) and its localization near the plaque-substrate interface have often prompted speculation that Mefp-5 plays a key role in adhesion. Using the surface forces apparatus, we show that on mica surfaces Mefp-5 achieves an adhesion energy approaching Ead = ~− 14 mJ/m2. This exceeds the adhesion energy of another interfacial protein, Mefp-3, by a factor of 4–5 and is greater than the adhesion between highly oriented monolayers of biotin and streptavidin. The adhesion to mica is notable for its dependence on Dopa, which is most stable under reducing conditions and acidic pH. Mefp-5 also exhibits strong protein-protein interactions with itself as well as with Mefp-3 from M. edulis.
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