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Effect of compressive force on unbinding specific protein-ligand complexes with force spectroscopy.

Publication ,  Journal Article
Bowers, CM; Carlson, DA; Rivera, M; Clark, RL; Toone, EJ
Published in: The journal of physical chemistry. B
May 2013

Atomic force microscopy (AFM) is used extensively for the investigation of noncovalent molecular association. Although the technique is used to derive various types of information, in almost all instances the frequency of complex formation, the magnitude of rupture forces, and the shape of the force-distance curve are used to determine the behavior of the system. We have used AFM to consider the effect of contact force on the unbinding profiles of lactose-galectin-3, as well as the control pairs lactose-KDPG aldolase, and mannose-galectin-3, where the interacting species show negligible solution-phase affinity. Increased contact forces (>250 pN) resulted in increased probabilitites of binding and decreased blocking efficiencies for the cognate ligand-receptor pair lactose-G3. Increased contact force applied to two control systems with no known affinity, mannose-G3 and lactose-KDPG aldolase, resulted in nonspecific ruptures that were indistinguishable from those of specific lactose-G3 interactions. These results demonstrate that careful experimental design is vital to the production of interpretable data, and suggest that contact force minimization is an effective technique for probing the unbinding forces and rupture lengths of only specific ligand-receptor interactions.

Duke Scholars

Published In

The journal of physical chemistry. B

DOI

EISSN

1520-5207

ISSN

1520-6106

Publication Date

May 2013

Volume

117

Issue

17

Start / End Page

4755 / 4762

Related Subject Headings

  • Silicon Compounds
  • Silicon
  • Recombinant Fusion Proteins
  • Oligopeptides
  • Microscopy, Atomic Force
  • Mice
  • Mannose
  • Lactose
  • Immobilized Proteins
  • Histidine
 

Citation

APA
Chicago
ICMJE
MLA
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Bowers, C. M., Carlson, D. A., Rivera, M., Clark, R. L., & Toone, E. J. (2013). Effect of compressive force on unbinding specific protein-ligand complexes with force spectroscopy. The Journal of Physical Chemistry. B, 117(17), 4755–4762. https://doi.org/10.1021/jp309393s
Bowers, Carleen M., David A. Carlson, Monica Rivera, Robert L. Clark, and Eric J. Toone. “Effect of compressive force on unbinding specific protein-ligand complexes with force spectroscopy.The Journal of Physical Chemistry. B 117, no. 17 (May 2013): 4755–62. https://doi.org/10.1021/jp309393s.
Bowers CM, Carlson DA, Rivera M, Clark RL, Toone EJ. Effect of compressive force on unbinding specific protein-ligand complexes with force spectroscopy. The journal of physical chemistry B. 2013 May;117(17):4755–62.
Bowers, Carleen M., et al. “Effect of compressive force on unbinding specific protein-ligand complexes with force spectroscopy.The Journal of Physical Chemistry. B, vol. 117, no. 17, May 2013, pp. 4755–62. Epmc, doi:10.1021/jp309393s.
Bowers CM, Carlson DA, Rivera M, Clark RL, Toone EJ. Effect of compressive force on unbinding specific protein-ligand complexes with force spectroscopy. The journal of physical chemistry B. 2013 May;117(17):4755–4762.

Published In

The journal of physical chemistry. B

DOI

EISSN

1520-5207

ISSN

1520-6106

Publication Date

May 2013

Volume

117

Issue

17

Start / End Page

4755 / 4762

Related Subject Headings

  • Silicon Compounds
  • Silicon
  • Recombinant Fusion Proteins
  • Oligopeptides
  • Microscopy, Atomic Force
  • Mice
  • Mannose
  • Lactose
  • Immobilized Proteins
  • Histidine