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Exploring Biomolecular Interaction Between the Molecular Chaperone Hsp90 and Its Client Protein Kinase Cdc37 using Field-Effect Biosensing Technology
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The Molecular Interaction Process.

Thomas M Laue1, Steven J Shire2

  • 1Molecular, Cellular and Biomedical Sciences, University of New Hampshire, Durham, New Hampshire 03824.

Journal of Pharmaceutical Sciences
|November 3, 2019
PubMed
Summary
This summary is machine-generated.

Noncovalent interactions are key to life and biopharmaceuticals, influencing both drug binding and formulation challenges. Understanding these thermodynamic processes helps manage protein aggregation and viscosity issues in drug development.

Keywords:
aggregationbindingbinding mechanismcolloidal stabilitymolecular interactionsmolecular stabilityphysical stabilityprotein-protein-interactionsviscosity

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Area of Science:

  • Biochemistry and Biophysics
  • Pharmaceutical Sciences
  • Chemical Engineering

Background:

  • Noncovalent molecular interactions are fundamental thermodynamic processes governing biological systems.
  • In biopharmaceuticals, these interactions are crucial for drug efficacy (target binding) but also cause manufacturing challenges like poor solubility and high viscosity.
  • Protein-protein interactions are a key focus, with principles applicable to all solution-based interactions.

Purpose of the Study:

  • To provide a foundational understanding of noncovalent interactions and their energetics.
  • To explore the interplay between protein and solvent properties in determining interaction energetics.
  • To elucidate the mechanisms behind protein aggregation, high viscosity, and emergent heterogeneity in biopharmaceutical formulations.

Main Methods:

  • The commentary synthesizes existing knowledge on noncovalent interaction pathways.
  • It analyzes the contributions of molecular and colloidal protein properties to interaction energetics.
  • A model is presented to explain how noncontacting interactions can lead to high viscosity without affecting solubility.

Main Results:

  • Noncovalent interactions follow common thermodynamic pathways.
  • Both protein and solvent properties significantly influence the energetics of these interactions.
  • Attractive interactions drive protein aggregation and viscosity, with emergent heterogeneity explaining high viscosity without low solubility.

Conclusions:

  • A comprehensive understanding of noncovalent interactions is vital for biopharmaceutical development.
  • The interplay of protein and solvent properties dictates interaction outcomes.
  • The presented model offers insights into managing viscosity and formulation challenges in protein-based drugs.