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Biotin Binding Hardly Affects Electron Transport Efficiency across Streptavidin Solid-State Junctions.

Sudipta Bera1, Sharada Govinda1, Jerry A Fereiro1,2

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|January 17, 2023
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Summary
This summary is machine-generated.

Electron transport (ETp) in protein junctions was studied using streptavidin (STV) and biotin. Ligand binding did not significantly alter ETp rates, despite causing minor structural changes in STV.

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Area of Science:

  • Biophysics
  • Materials Science
  • Protein Electronics

Background:

  • Electron transport (ETp) efficiency in solid-state junctions is often enhanced by electron-rich cofactors.
  • Investigating cofactor-free proteins is crucial for understanding intrinsic ETp mechanisms.

Purpose of the Study:

  • To investigate meso-scale electron transport (ETp) through streptavidin (STV) monolayers.
  • To determine if biotin binding, which induces structural changes, affects ETp rates in STV.

Main Methods:

  • Fabrication of gold nanowire-electrode-STV monolayer-microelectrode junctions.
  • Measurement of ETp across native and thiolated STV monolayers.
  • Analysis of temperature dependence of ETp over the 80–300 K range.

Main Results:

  • No statistically significant change in conductance was observed between free STV and biotin-bound STV.
  • A slight, unusual negative temperature dependence of ETp was noted towards room temperature.
  • This temperature dependence is attributed to reversible structural shrinkage of STV below 160 K.

Conclusions:

  • Ligand binding to streptavidin does not significantly impact electron transport rates across STV monolayers.
  • The observed temperature dependence suggests unique structural dynamics influencing electron transport in STV films.