ArticleThe journal of physical chemistry letters2019
Surface-Templated Nanobubbles Protect Proteins from Surface-Mediated Denaturation.
Article in The journal of physical chemistry letters, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.
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Who cites it
3 citing papers in PubMed, 10 citations in OpenAlex.
- Effect of Organic Compounds and Alkalinity on the Stability of Bulk Nanobubbles: A Molecular Dynamics Study.Molecules (Basel, Switzerland) · 2025Article
- The Influence of Air Nanobubbles on Controlling the Synthesis of Calcium Carbonate Crystals.Materials (Basel, Switzerland) · 2022Article
- Faster Surface Ligation Reactions Improve Immobilized Enzyme Structure and Activity.Journal of the American Chemical Society · 2021Article
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Authors and funding
9 authors at 1 institution in 1 country.
Funding
Abstract
In this Letter, we report that surface-bound nanobubbles reduce protein denaturation on methylated glass by irreversible protein shell formation. Single-molecule total internal reflection fluorescence (SM-TIRF) microscopy was combined with intramolecular Förster resonance energy transfer (FRET) to study the conformational dynamics of nitroreductase (NfsB) on nanobubble-laden methylated glass surfaces, using reflection brightfield microscopy to register nanobubble locations with NfsB adsorption. First, NfsB adsorbed irreversibly to nanobubbles with no apparent desorption after 5 h. Moreover, virtually all (96%) of the NfsB molecules that interacted with nanobubbles remained folded, whereas less than 50% of NfsB molecules remained folded in the absence of nanobubbles on unmodified silica or methylated glass surfaces. This trend was confirmed by ensemble-average fluorometer TIRF experiments. We hypothesize that nanobubbles reduce protein damage by passivating strongly denaturing topographical surface defects. Thus, nanobubble stabilization on surfaces may have important implications for antifouling surfaces and improving therapeutic protein storage.
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