Abstract
Background: Human serum albumin (HSA) is the most abundant protein in human serum. It has numerous functions, one of which is transport of small hydrophobic molecules, including drugs, toxins, nutrients, hormones and metabolites. HSA has the ability to interact with a wide variety of structurally different compounds. This promiscuous, nonspecific affinity can lead to sudden changes in concentrations caused by displacement, when two or more compounds compete for binding to the same molecular site.
Objective: It is important to consider drug combinations and their binding to HSA when defining dosing regimens, as this can directly influence drug’s free, active concentration in blood. Conclusion: In present paper we review drug interactions with potential for displacement from HSA, situations in which they are likely to occur and their clinical significance. We also offer guidelines in designing drugs with decreased binding to HSA.Keywords: Human serum albumin, drug displacement, pharmacokinetic interactions, free concentration, drug design, Sudlow’s site I, Sudlow’s site II.
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