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Covalent Attachment of Single Molecules for AFM-based Force Spectroscopy
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Correction of systematic errors in single-molecule force spectroscopy with polymeric tethers by atomic force

Chad Ray1, Jason R Brown, Boris B Akhremitchev

  • 1Department of Chemistry, Duke University, Durham, North Carolina 27708, USA.

The Journal of Physical Chemistry. B
|February 8, 2007
PubMed
Summary

This study introduces a new analytical model to correct systematic errors in single-molecule force spectroscopy data. The model accounts for polymer tether elasticity, improving the accuracy of dissociation rates and barrier width measurements in atomic force microscopy experiments.

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Area of Science:

  • Biophysics
  • Physical Chemistry
  • Materials Science

Background:

  • Single-molecule force spectroscopy, particularly using atomic force microscopy (AFM), is crucial for studying molecular interactions.
  • The Bell-Evans model is standard for analyzing rupture forces, often assuming a constant loading rate.
  • Inconsistencies arise in AFM data analysis due to variations in probe velocity and loading rate, and the influence of polymer tether stiffness.

Purpose of the Study:

  • To develop an analytical model that corrects systematic errors in force spectroscopy parameters caused by nonlinear loading from polymer tethers.
  • To provide analytical expressions for systematic errors in common data reduction procedures.
  • To analyze and correct experimental data from hydrophobic bond dissociation experiments.

Main Methods:

  • Developed an analytical model integrating the Bell-Evans model with asymptotic tether stretching models.
  • Analyzed two common data reduction procedures to derive expressions for systematic errors.
  • Applied the model, based on the freely jointed chain model, to correct experimental AFM data of hexadecane molecule dissociation.

Main Results:

  • The model reveals that barrier width is underestimated and dissociation rates are overestimated when polymer tether elasticity is ignored.
  • Analytical expressions for systematic errors are provided for freely jointed chain and wormlike chain polymer models.
  • Correction of experimental data reduced data spread and increased the measured barrier width to 0.43 nm.

Conclusions:

  • Accounting for polymer tether elasticity is essential for accurate force spectroscopy analysis.
  • The developed model provides a method to correct systematic errors, enhancing the reliability of biophysical measurements.
  • The corrected results suggest a barrier width consistent with theoretical predictions of hydrophobic dewetting.