Interactions of nanobubbles with bovine serum albumin and papain films on gold surfaces
Language English Country United States Media print
Document type Journal Article, Research Support, Non-U.S. Gov't
PubMed
22239809
DOI
10.1116/1.3650300
Knihovny.cz E-resources
- MeSH
- Ethanol chemistry MeSH
- Nanostructures chemistry MeSH
- Papain metabolism MeSH
- Surface Properties MeSH
- Serum Albumin, Bovine metabolism MeSH
- Cattle MeSH
- Water chemistry MeSH
- Gold metabolism MeSH
- Animals MeSH
- Check Tag
- Cattle MeSH
- Animals MeSH
- Publication type
- Journal Article MeSH
- Research Support, Non-U.S. Gov't MeSH
- Names of Substances
- Ethanol MeSH
- Papain MeSH
- Serum Albumin, Bovine MeSH
- Water MeSH
- Gold MeSH
Nanobubbles formed on monocrystalline gold/water interface by means of the ethanol-to-water solvent exchange were exposed to the solutions of either bovine serum albumin or papain proteins. Both proteins do not change the position of nanobubbles in water, as observed by in situ tapping mode atomic force microscopy imaging before and after the introduction of the protein. The aqueous environment was subsequently replaced by ethanol. While all nanobubbles were found to dissolve in ethanol in the presence of bovine serum albumin, most of them survived when papain was employed. The protective ability of papain was ascribed to its resistance towards the protein denaturation in aqueous solutions of ethanol. The authors employed in situ atomic force nanolithography to investigate the nanomorphology of the papain/nanobubble assemblies in ethanol.
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