Effect of Protein Adsorption on Air Plastron Behavior of a Superhydrophobic Surface

被引:15
作者
Wang, Yujie [1 ,2 ]
Zhang, Boce [5 ]
Dodiuk, Hanna [1 ,3 ]
Kenig, Shmuel [1 ,3 ]
Barry, Carol [1 ]
Ratto, JoAnn [4 ]
Mead, Joey [1 ]
Jia, Zhen [5 ]
Turkoglu, Sevil [1 ]
Zhang, Jinde [1 ]
机构
[1] Univ Massachusetts, Dept Plast Engn, Lowell, MA 01854 USA
[2] Univ Massachusetts, Biomed Engn & Biotechnol Program, Lowell, MA 01854 USA
[3] Shenkar Coll Engn Design & Art, Polymer Mat Engn Dept, Pernick Fac Engn, IL-5211401 Ramat Gan, Israel
[4] US Army, Combat Capabil Dev Command Soldier Ctr DEVCOM Sol, Natick, MA 01760 USA
[5] Univ Florida, Dept Food Sci & Human Nutr, Gainesville, FL 32611 USA
关键词
nanocomposite coating; superhydrophobicity; air plastron; protein adsorption; Cassie-Baxter/Wenzel transition; SELF-ASSEMBLED MONOLAYERS; BACTERIAL ADHESION; RESISTANCE; WATER; TRANSITIONS; DROPLETS;
D O I
10.1021/acsami.1c15981
中图分类号
TB3 [工程材料学];
学科分类号
0805 ; 080502 ;
摘要
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.
引用
收藏
页码:58096 / 58103
页数:8
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