Nuclear relaxation studies in ligand-macromolecule affinity index determinations

Comparison of the binding affinity of chlorogenic acid with two serum albumins

“…This parameter is constant at fixed temperature and ligand concentration, and can be used to gain an insight into the dynamics of the ligand-receptor interaction process, and particularly, to compare the strength of the interaction process involving the same ligand and different proteins [24,25].…”

“…Diffusion methods can provide useful information about ligand-receptor interactions, the binding can be characterized by significant changes in the ligand diffusion coefficient [22,23]. However, in the present work, the affinity index is used due to its specific ability to compare the strength of the interaction process involving the same ligand and different proteins [24,25]. Molecular docking is a powerful computer-aided drug design approach which can be used to predict the orientation of small molecules to their target proteins.…”

Combined use of nuclear magnetic resonance and infrared spectroscopy for studying recognition processes between amphenicolic antibiotics and albumin

“…33 The affinity index calculated from proton-selective relaxation rates provides a deeper knowledge of the dynamics of the ligand-macromolecule interaction process, and offers several advantages. It is calculated as the slope of a straight line passing through the origin and is less affected by intrinsic errors than the intercept calculation.…”

“…33 The affinity index is a constant if the temperature and ligand concentration are specified, as suggested by the T and L indices on the affinity index term.…”

Ligand–macromolecule complexes: affinity index determination by selective nuclear relaxation analysis

“…A parameter, the 'affinity index,' calculated at constant temperature and constant ligand concentration, was defined and used to characterize the overall recognition process between ligands and macromolecules. 11,12 The affinity index can be calculated in systems dominated by fast chemical exchange of a ligand between the free and bulk conditions, as often occurs in ligand-bioreceptor recognition processes.…”