Kinetic binding rate constants, together with equilibrium constants, provide a complete view of molecular recognition. In addition, modeling ligand-receptor binding/unbinding pathways can provide insights into molecular association, including intermolecular interactions, changes of solvent and solute entropy, barriers to binding, and conformational changes in the intermediate states. This presentation discusses the complete binding enthalpy and entropy profiles of both solute and solvent. We applied MD simulations for multiple guests binding to beta-cyclodextrin to compute binding enthalpy, entropy, and rate constants. The free energy profile using umbrella sampling methods will also be discussed. The importance in solvent effects, and the sensitivity of use of different force fields to model conformational flexibility will be discussed as well. The results also raise questions about how to use computed thermodynamic and kinetic values to validate our force field parameters.                                                                 <br/>

Modeling ligand-receptor binding thermodynamics and kinetics: Comprehensive picture of molecular recognition

Macromolecular Chemistry: The Second Century

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ACS Spring 2020 National Meeting & Expo

The official archive and repository for all ACS Meetings & Expositions abstracts and select posters or presentations.