In recent decades, drug-protein interactions have been widely studied and several methods of analysis
of these phenomena have been developed and improved. These can be classified into separation, physical, chromatographic
and electrophoretic methods. This review depicts the assumptions and mechanisms of methods from
each group, details their strengths and weaknesses, and presents examples of their usage from the literature. Equilibrium
dialysis, ultrafiltration, Hummel-Dreyer method or high performance affinity chromatography are given
as representative examples, but this issue is far more expanded. Nowadays, increasing attention is paid to the
computational methods and molecular modeling which are convenient tools to estimate protein binding affinity
based on the physicochemical properties of compounds. To gain a broader overview, the study also examines the
protein binding ability and pharmacotherapy of drugs against a range of substrates such as plasma, skin, tissue
and human milk.
Keywords: Drug-protein binding, protein binding analysis, computational modeling, human serum albumin, alpha-1-acid glycoprotein,
quantitative structure-activity relationship.
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