Journal
SCIENCE
Volume 349, Issue 6248, Pages 625-628Publisher
AMER ASSOC ADVANCEMENT SCIENCE
DOI: 10.1126/science.aab3175
Keywords
-
Categories
Funding
- Institute for Basic Science [IBS-R011-D1]
- National Research Foundation of Korea (NRF) [NRF-2014R1A1A2056386]
- NRF [2013R1A1A1008025, NRF-2005-0093845]
- Ministry of Science, ICT & Future Planning, Republic of Korea [IBS-R011-D1-2015-A00] Funding Source: Korea Institute of Science & Technology Information (KISTI), National Science & Technology Information Service (NTIS)
- National Research Foundation of Korea [2013R1A1A1008025] Funding Source: Korea Institute of Science & Technology Information (KISTI), National Science & Technology Information Service (NTIS)
Ask authors/readers for more resources
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 bymussels. 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.
Authors
I am an author on this paper
Click your name to claim this paper and add it to your profile.
Reviews
Recommended
No Data Available