赖氨酸
儿茶酚
粘附
化学
铁载体
盐(化学)
聚合物
生物化学
氨基酸
生物物理学
有机化学
生物
基因
作者
Greg P. Maier,M. Rapp,J. Herbert Waite,Jacob N. Israelachvili,Alison Butler
出处
期刊:Science
[American Association for the Advancement of Science (AAAS)]
日期:2015-08-07
卷期号:349 (6248): 628-632
被引量:550
标识
DOI:10.1126/science.aab0556
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.
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