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2011 ; 2
(6
): 433-7
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Thermodynamics of ligand binding and efficiency
#MMPMID24900326
Reynolds CH
; Holloway MK
ACS Med Chem Lett
2011[Jun]; 2
(6
): 433-7
PMID24900326
show ga
Analysis of the experimental binding thermodynamics for approximately 100
protein-ligand complexes provides important insights into the factors governing
ligand affinity and efficiency. The commonly accepted correlation between
enthalpy and -T?S is clearly observed for this relatively diverse data set. It is
also clear that affinity (i.e., ?G) is not generally correlated to either
enthalpy or -T?S. This is a worrisome trend since the vast majority of
computational structure-based design is carried out using interaction energies
for one, or at most a few, ligand poses. As such, these energies are most closely
comparable to enthalpies not free energies. Closer inspection of the data shows
that in a few cases the enthalpy (or -T?S) is correlated with free energy. It is
tempting to speculate that this could be an important consideration as to why
some targets are readily amenable to modeling and others are not. Additionally,
analysis of the enthalpy and -T?S efficiencies shows that the trends observed for
ligand efficiencies with respect to molecular size are primarily a consequence of
enthalpic, not entropic, effects.
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