Biotinylated indoles were prepared for application as bifunctional probes for the detection of indolebinding proteins which participate in the life processes of humans, animals, plants, and bacteria. The indole nucleus was functionalized, at ring positions 3, 5, or 6, by attachment of a 2-aminoethyl group, which was then coupled to the carboxyl moiety of biotin, via a spacer composed of 3 or 4 concatenated â-alanine residues. The constructs thus obtained were able to inhibit tryptophanase activity, similarly to indole in a concentration-dependent manner. They also bound strongly to lysozyme and weakly to bovine and human serum albumins, in accordance with the known affinities of these proteins for indole and 3-(2-aminoethyl)indole (tryptamine). The biotin end of the protein-bound bifunctional probes could then be detected by coupling to (strept)avidin conjugated to alkaline phosphatase or horseradish peroxidase, followed by incubation with substrates which are converted by these enzymes to intensely colored or chemiluminescent products.
|Number of pages||11|
|Publication status||Published - 2001|
|Event||Xth Conference on organic chemistry and biochemistry of young scientists - Liblice Castle, Czech Republic|
Duration: 15 Jun 1998 → …
Dolusic, E., Kowalczyk, M., Magnus, V., Sandberg, G., & Normanly, J. (2001). Biotinylated indoles as probes for indole-binding proteins. Bioconjugate Chemistry, 12(2), 152-162. https://doi.org/10.1021/bc000035o