Binding behavior of amino acid conjugates of indole-3-acetic acid to immobilized human serum albumin.

The affinity of indole-3-acetic acid (IAA), indole-3-propionic acid, indole-3-butyric acid and 24 of their amino acid conjugates to immobilized human serum albumin, as expressed by the retention factor k (determined by HPLC), was dependent on (1) lipophilicity, (2) chirality and (3) functional groups in the amino acid moiety; in some cases conformation plays an additional role. Two lipophilicity-related parameters afforded quantitative correlations with k: retention on a C18 reversed-phase column (experimental approach) and the distance between the hydrophilic and hydrophobic poles of the molecules (in silico approach). Most compounds examined are possible metabolic precursors of IAA, an experimental tumor therapeutic.