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.
D000478:Alkylation; D001665:Binding Sites / Q000187:drug effects*; D001667:Binding, Competitive / Q000187:drug effects; D055598:Chemical Phenomena; D002621:Chemistry; D006801:Humans; D007211:Indoles / Q000378:metabolism*; D007213:Indomethacin / Q000031:analogs & derivatives* / Q000494:pharmacology; D007700:Kinetics; D011485:Protein Binding / Q000187:drug effects; D012709:Serum Albumin / Q000378:metabolism; D014364:Tryptophan / Q000097:blood
D007211:Indoles; D012709:Serum Albumin; D014364:Tryptophan; D007213:Indomethacin