Naslov
Biotinylated indoles as probes for indole-binding proteins

Autori
Dolušić, Eduard ; Kowalczyk, Mariusz ; Magnus, Volker ; Sandberg, Göran ; Normanly, Jennifer

Izvornik
Bioconjugate chemistry (1043-1802) 12 (2001), 2; 152-162

Vrsta, podvrsta i kategorija rada
Radovi u časopisima, članak, znanstveni

Ključne riječi
bifunctional probe; indole; biotin; indole-binding protein; tryptophanase; lysozyme; serum albumin; avidin-enzyme conjugate

Sažetak
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 beta-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.

Izvorni jezik
Engleski

Znanstvena područja
Kemija

POVEZANOST RADA