BINDING OF RETINOID ANALOGS TO ALBUMIN AND LIPOPROTEINS OF HUMAN PLASMA

The interactions of ten retinoid derivatives with human serum albumin (HSA) and lipoproteins have been investigated in vitro by an erythrocy te-partitioning technique that allows a quantitative estimation of the protein and erythrocyte binding. it was found that ail these compound s were highly bound to HSA and lipoprotein. The binding to HSA was sup erior or similar to the binding to lipoprotein in the case oi carboxyl ic acid derivatives. For the neutral derivatives, the binding to lipop roteins was generally higher than the binding to HSA. Retinoid binding to lipoproteins was strongly related to the computed octanol/water pa rtition coefficient (CLOGP).