Kinetic And Thermodynamic Principles Underlying Drug–Target Interactions: A Review Article

Abstract

All drugs interact with their biological targets. The nature of the thermodynamic and kinetic laws of such interactions is what needs to be well known for subsequent discovery of new drugs and modern design. Thermodynamic affinity, enthalpy, and entropy parameters describe the strengths and stabilities of drug-target complexes; kinetic parameters describe how rapidly binding occurs as well as for how long the interaction takes place most often expressed "on/off" rates (kon/koff). "Recent years have seen a shift in focus towards kinetic behavior, more specifically residence time which has emerged as an excellent indicator of a drug's efficacy within living organisms." "It acquires high relevance particularly in the case of large biopharmaceuticals like monoclonal antibodies, peptides, and nucleic acid-based therapeutics since they have broad binding surfaces due to which there is a need for careful control over interaction dynamics."

Keywords:

Kinetics, Thermodynamics, Drug–target interactions

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