Biotinylated Indoles as Probes for Indole-Binding Proteins. Dolušić, E., Kowalczyk, M., Magnus, V., Sandberg, G., & Normanly, J. Bioconjugate Chemistry, 12(2):152–162, March, 2001. Publisher: American Chemical Society![Biotinylated Indoles as Probes for Indole-Binding Proteins [link]](https://bibbase.org/img/filetypes/link.svg "link")
Paper doi abstract bibtex Biotinylated indoles were prepared for application as bifunctional probes for the detection of indole-binding 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 β-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.
@article{dolusic_biotinylated_2001,
title = {Biotinylated {Indoles} as {Probes} for {Indole}-{Binding} {Proteins}},
volume = {12},
issn = {1043-1802},
url = {https://doi.org/10.1021/bc000035o},
doi = {10/dmdv93},
abstract = {Biotinylated indoles were prepared for application as bifunctional probes for the detection of indole-binding 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 β-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 = {2},
urldate = {2021-11-02},
journal = {Bioconjugate Chemistry},
author = {Dolušić, Eduard and Kowalczyk, Mariusz and Magnus, Volker and Sandberg, Göran and Normanly, Jennifer},
month = mar,
year = {2001},
note = {Publisher: American Chemical Society},
pages = {152--162},
}
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