CommentaryDo thermodynamic studies provide information on both the binding to and the activation of dopaminergic and other receptors?
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Cited by (57)
Enthalpy-entropy compensation for some drugs dissociation in aqueous solutions
2012, Fluid Phase EquilibriaCitation Excerpt :In fact, the standard enthalpy ΔH0 can be considered a quantitative indicator of the changes in intermolecular bond energies (hydrogen bonding and Van der Waals interactions) occurring during the binding, while the standard entropy ΔS0 is most likely a good indicator of the rearrangements undergone by the water molecules during the same process. Methods based on pKa measurements over a range of temperatures combined with Van’t Hoff plots have been successfully applied, as discussed in recent critical appraisals [52–54]. The negative value of ΔS0 is due to the increased order.
Binding thermodynamics at the human cannabinoid CB<inf>1</inf> and CB<inf>2</inf> receptors
2010, Biochemical PharmacologyCitation Excerpt :Such a method has proved to be successful in many cases. Until now, elegant studies have been carried out on several receptor systems, demonstrating the value of thermodynamics for investigating receptor–ligand interactions [3,4]. In addition, some of these studies have suggested that measurement of thermodynamic parameters can allow the discrimination of agonist and antagonist ligands.
Thermodynamics of A<inf>2B</inf> adenosine receptor binding discriminates agonistic from antagonistic behaviour
2008, Biochemical PharmacologyCitation Excerpt :In this light we suggest that the similarity in thermodynamic parameters probably reflects a common mechanism of ligand–receptor interaction for all adenosine receptors subtypes and this may explain the difficulty to obtain selective adenosine ligands. However the development of therapeutic substances has been strongly advanced by rational drug design, which involves achieving full understanding of a given biomolecular interaction by combining structural, kinetic and thermodynamic information [32–35]. Therefore, the availability of thermodynamic data adds important information to the decision-making process in drug development [36,37].
Serum albumins have five sites for binding of cationic dendrimers
2007, Biochimica et Biophysica Acta - Proteins and ProteomicsStudy on the thermodynamic characteristics between fluoroquinolone and bovine serum albumin
2007, Journal of Chemical ThermodynamicsActivation of ionotropic receptors and thermodynamics of binding
2005, Neurochemistry International