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High-affinity drug binding involves parallel induced-fit and conformational selection pathways, influenced by ligand concentration. New flux-based methods reveal these dynamics in physiological, nonequilibrium conditions.

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Area of Science:

  • Biochemistry
  • Pharmacology
  • Chemical Biology

Background:

  • Historically, high-affinity drug binding was attributed primarily to the induced-fit pathway.
  • Recent binding flux-based approaches suggest induced-fit and conformational selection pathways operate in parallel.
  • The relative contribution of these pathways is concentration-dependent, particularly under equilibrium conditions.

Purpose of the Study:

  • To highlight the importance of extending binding flux-based approaches to physiological nonequilibrium conditions.
  • To demonstrate the application of these methods in understanding ligand-target complex formation in vivo.
  • To analyze transient experimental data within a conventional thermodynamic cycle framework.

Main Methods:

  • Utilizing binding flux-based approaches to analyze drug-target interactions.
  • Investigating ligand-target complex formation under both equilibrium and nonequilibrium conditions.
  • Applying thermodynamic cycle analysis to experimental data.

Main Results:

  • Both induced-fit and conformational selection pathways contribute to high-affinity drug binding.
  • The balance between these pathways is modulated by ligand concentration.
  • Flux-based approaches reveal dynamic binding processes relevant to physiological conditions.

Conclusions:

  • Binding flux methods offer valuable insights into drug-target interactions beyond equilibrium binding.
  • Understanding parallel binding pathways is crucial for comprehending drug efficacy in vivo.
  • Transient binding events can be effectively analyzed using thermodynamic cycle principles.