Thermodynamic aspects of drug-receptor interactions

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Abstract

Determination of whether a specific ligand-receptor interaction at equilibrium is enthalpy- and/or entropy-stabilized can be achieved by thermodynamic analysis, writes Robert Hitzemann. Enthalpy stabilization is usually associated with the formation of new bonds (e.g. hydrogen bonds and van der Waal's interactions) in the ligand-receptor-membrane array, whereas entropy stabilization is usually characterized by the displacement of ordered water molecules coupled to the formation of new hydrophobic interactions. The initial step in the receptor association is generally entropy stabilized. For some agonists and antagonists, this initial step is followed by one or more steps that are enthalpy stabilized. Interestingly, there is a wide diversity in the thermodynamics of agonist/ antagonist receptor binding, suggesting several different mechanisms of information transfer.

Original languageEnglish (US)
Pages (from-to)408-411
Number of pages4
JournalTrends in Pharmacological Sciences
Volume9
Issue number11
DOIs
StatePublished - 1988
Externally publishedYes

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Drug Receptors
Entropy
Drug Interactions
Thermodynamics
Enthalpy
Stabilization
Ligands
Hydrophobic and Hydrophilic Interactions
Hydrogen
Hydrogen bonds
Association reactions
Membranes
Molecules
Water

ASJC Scopus subject areas

  • Pharmacology
  • Toxicology

Cite this

Thermodynamic aspects of drug-receptor interactions. / Hitzemann, Robert.

In: Trends in Pharmacological Sciences, Vol. 9, No. 11, 1988, p. 408-411.

Research output: Contribution to journalArticle

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