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Updated: Jul 1, 2026
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Encapsulating Cytochrome c in Silica Aerogel Nanoarchitectures without Metal Nanoparticles while Retaining Gas-phase Bioactivity
Published on: March 1, 2016
Early structural evolution of native cytochrome c after solvent removal.
Michal Z Steinberg1, Ron Elber, Fred W McLafferty
1Department of Physical Chemistry, Fritz Haber Research Center, Hebrew University, Jerusalem 91904, Israel.
Chembiochem : a European Journal of Chemical Biology
|September 13, 2008
Summary
Electrospray ionization moves proteins into the gas phase. Computational data show proteins rapidly form new noncovalent bonds after solvent removal, maintaining their overall structure.
Area of Science:
- Biochemistry
- Physical Chemistry
- Computational Biology
Background:
- Electrospray ionization (ESI) is crucial for transferring biomolecules like proteins from solution to the gas phase for mass spectrometry analysis.
- While covalent bonds are generally stable during ESI, the impact of solvent removal on noncovalent interactions within proteins remains less understood.
Purpose of the Study:
- To investigate the immediate structural rearrangements of native cytochrome c following desolvation using atomic-level computational simulations.
- To determine the timescale and nature of structural changes, particularly the stability of noncovalent bonds, after solvent removal.
Main Methods:
- Atomistic molecular dynamics simulations were employed to model cytochrome c immediately after desolvation.
- The simulations covered a time segment of up to 4.2 nanoseconds, focusing on structural changes and noncovalent bond dynamics.
- Results were compared with experimental data from native electron capture dissociation (ECD) experiments.
Main Results:
- Significant structural changes, including the formation of new noncovalent bonds, were observed as early as picoseconds after desolvation.
- No significant breaking of native noncovalent bonds occurred within the simulated 4.2 ns timeframe.
- The protein's global fold remained largely consistent with its solution state, with transient stabilization via new noncovalent interactions involving charged surface residues.
Conclusions:
- The gas-phase environment post-ESI does not immediately disrupt native noncovalent interactions in proteins; instead, it can lead to the formation of new stabilizing interactions.
- Computational predictions align with experimental findings from native ECD, supporting the proposed mechanisms of structural stabilization.
- Global structural rearrangements occur on a much longer timescale (milliseconds) than captured by the picosecond to nanosecond simulations.
