Use of a Human Serum Albumin-Based Stationary Phase for High-Performance Liquid Chromatography as a Tool for the Rapid Determination of Drug–Plasma Protein Binding

Evaluating the binding selectivity of transthyretin amyloid fibril inhibitors in blood plasma

“…These methods provide information on the amount of compound bound to total plasma protein, but they do not identify the specific target. Drug binding to isolated or recombinant plasma proteins can be characterized by numerous methods such as fluorescence (58), NMR (59), CD or related spectroscopies (60), chromatography (61,62), calorimetry (37), or surface plasmon resonance (63). While these methods provide the binding affinity to the suspected plasma protein target, typically albumin for acidic drugs, or ␣ 1 -acid glycoprotein for basic drugs (64), they do not predict the extent of binding in a biological fluid because the competitive proteins and small molecules are generally unknown.…”

Fast Gradient HPLC Method to Determine Compounds Binding to Human Serum Albumin. Relationships with Octanol/Water and Immobilized Artificial Membrane Lipophilicity

“…Several attempts have been made to set up quantitative structure-binding relationships for HSA binding, 12,13 and they have revealed the positive contributions of lipophilicity, the presence of aromatic substituents, and presence of carboxylic acids in strong HSA binding.…”

Application of High Performance Liquid Chromatography for the Measurements of Lipophilicity and Biomimetic Binding Properties in Drug Discovery

“…Several authors presented good correlations between the logarithmic retention factors measured on the HSA stationary phase and plasma protein binding of drugs obtained by equilibrium dialysis or ultra-filtration methods [43][44][45][46]. The principles of using immobilised target bio-polymers to measure drug affinity by HPLC have been reviewed by Bertucci et al [47].…”