Functional modification of indole binding site with indomethacin congeners

Indomethacin and four congeners were shown by equilibrium dialysis to interfere with the binding of L-tryptophan at the primary indole binding site on defatted human serum albumin. Incubation of albumin with 1-(p-bromoacetamidobenzovl)- and 1-(m-bromoacetamidobenzoyl)-5-methoxy-2-methyl-3-indolylacetic acid functionally modified this site, decreasing the availability of the site for the binding of L-tryptophan. Incubation in the presence of a large excess of L-tryptophan resulted in the partial protection of the site from modification by 1-(m-bromoacetamidobenzoyl)-5-methoxy-2-methyl-3-indolylacetic acid.