Adaptive synergy between catechol and lysine promotes wet adhesion by surface salt displacement

被引:600
作者
Maier, Greg P. [1 ]
Rapp, Michael V. [2 ]
Waite, J. Herbert [3 ]
Israelachvili, Jacob N. [2 ,4 ]
Butler, Alison [1 ]
机构
[1] Univ Calif Santa Barbara, Dept Chem & Biochem, Santa Barbara, CA 93106 USA
[2] Univ Calif Santa Barbara, Dept Chem Engn, Santa Barbara, CA 93106 USA
[3] Univ Calif Santa Barbara, Mol Cellular & Dev Biol, Santa Barbara, CA 93106 USA
[4] Univ Calif Santa Barbara, Mat Dept, Santa Barbara, CA 93106 USA
基金
美国国家科学基金会;
关键词
MUSSEL; PROTEINS; ENTEROBACTIN; HYDRATION; POLYMERS; COATINGS; PH;
D O I
10.1126/science.aab0556
中图分类号
O [数理科学和化学]; P [天文学、地球科学]; Q [生物科学]; N [自然科学总论];
学科分类号
07 ; 0710 ; 09 ;
摘要
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.
引用
收藏
页码:628 / 632
页数:5
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