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Surface-Templated Nanobubbles Protect Proteins from Surface-Mediated Denaturation.

David S Bull¹, Daniel F Kienle¹, Andres F Chaparro Sosa¹

¹Department of Chemical and Biological Engineering , University of Colorado Boulder , Boulder , Colorado 80303 , United States.

The Journal of Physical Chemistry Letters

|May 9, 2019

Summary

Surface nanobubbles prevent protein unfolding by forming protective shells. This discovery offers potential for improved protein storage and antifouling surfaces.

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Area of Science:

Biophysics
Surface Science
Materials Science

Background:

Protein denaturation on surfaces is a significant challenge in biotechnology and medicine.
Surface-bound nanobubbles are an emerging phenomenon with potential applications.

Purpose of the Study:

To investigate the effect of surface nanobubbles on protein denaturation.
To understand the mechanism by which nanobubbles influence protein conformational stability.

Main Methods:

Utilized single-molecule total internal reflection fluorescence (SM-TIRF) microscopy.
Employed intramolecular Förster resonance energy transfer (FRET) to monitor protein dynamics.
Combined with reflection brightfield microscopy to localize nanobubbles and protein adsorption.

Main Results:

Nitroreductase (NfsB) adsorbed irreversibly to nanobubbles, with no desorption observed over 5 hours.
Virtually all (96%) NfsB molecules interacting with nanobubbles remained folded.
In contrast, less than 50% of NfsB molecules remained folded on surfaces without nanobubbles.

Conclusions:

Surface nanobubbles significantly reduce protein denaturation by forming irreversible protein shells.
Nanobubbles likely passivate denaturing surface defects, preserving protein structure.
Nanobubble stabilization on surfaces holds promise for antifouling applications and therapeutic protein storage.