Journal
ACS APPLIED MATERIALS & INTERFACES
Volume 13, Issue 48, Pages 58096-58103Publisher
AMER CHEMICAL SOC
DOI: 10.1021/acsami.1c15981
Keywords
nanocomposite coating; superhydrophobicity; air plastron; protein adsorption; Cassie-Baxter/Wenzel transition
Funding
- US Army's Combat Capabilities Development Command Soldier Center [PR2021_80294]
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This study found that protein solutions significantly weaken the stability of air plastron (AP) on superhydrophobic (SHP) materials, mainly due to the surface tension of protein solutions and protein adsorption on SHP substrates.
Protein fouling on critical biointerfaces causes significant public health and clinical ramifications. Multiple strategies, including superhydrophobic (SHP) surfaces and coatings, have been explored to mitigate protein adsorption on solid surfaces. SHP materials with underwater air plastron (AP) layers hold great promise by physically reducing the contact area between a substrate and protein molecules. However, sustaining AP stability or lifetime is crucial in determining the durability and long-term applications of SHP materials. This work investigated the effect of protein on the AP stability using model SHP substrates, which were prepared from a mixture of silica nanoparticles and epoxy. The AP stability was determined using a submersion test with real-time visualization. The results showed that AP stability was significantly weakened by protein solutions compared to water, which could be attributed to the surface tension of protein solutions and protein adsorption on SHP substrates. The results were further examined to reveal the correlation between protein fouling and accelerated AP dissipation on SHP materials by confocal fluorescent imaging, surface energy measurement, and surface robustness modeling of the Cassie-Baxter to Wenzel transition. The study reveals fundamental protein adsorption mechanisms on SHP materials, which could guide future SHP material design to better mitigate protein fouling on critical biointerfaces.
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