Energy landscape roughness of the streptavidin-biotin interaction

Félix Rico, Vincent T. Moy

Research output: Contribution to journalArticle

67 Citations (Scopus)

Abstract

Molecular interactions between receptors and ligands can be characterized by their free energy landscape. In its simplest representation, the energy landscape is described by a barrier of certain height and width that determines the dissociation rate of the complex, as well as its dynamic strength. Some interactions, however, require a more complex landscape with additional barriers and roughness along the reaction coordinate. This roughness slows down the dissociation kinetics of the interaction and contributes to its dynamic strength. The streptavidin-biotin complex has been extensively studied due to its remarkably low dissociation kinetics. However, single molecule measurements from independent experiments showed scattered and disparate results. In this work, the energy landscape roughness of the streptavidin-biotin interaction was estimated to be in the range of 5-8kBT using dynamic force spectroscopy (DFS) measurements at three different temperatures. These results can be used to explain both its slow dissociation kinetics and the discrepancies in the reported force measurements.

Original languageEnglish
Pages (from-to)495-501
Number of pages7
JournalJournal of Molecular Recognition
Volume20
Issue number6
DOIs
StatePublished - Nov 1 2007

Fingerprint

Streptavidin
Biotin
Surface roughness
Kinetics
Molecular interactions
Force measurement
Spectrum Analysis
Free energy
Ligands
Temperature
Spectroscopy
Molecules
Experiments

Keywords

  • Atomic force microscopy
  • Dynamic force spectroscopy
  • Energy landscape
  • Energy landscape roughness
  • Energy surface
  • Free energy
  • Streptavidin-biotin
  • Temperature

ASJC Scopus subject areas

  • Biochemistry
  • Genetics
  • Computer Vision and Pattern Recognition
  • Immunology
  • Molecular Biology
  • Structural Biology

Cite this

Energy landscape roughness of the streptavidin-biotin interaction. / Rico, Félix; Moy, Vincent T.

In: Journal of Molecular Recognition, Vol. 20, No. 6, 01.11.2007, p. 495-501.

Research output: Contribution to journalArticle

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