Atropisomerism in 3,4,5-Tri-(2-methoxyphenyl)-2,6-lutidine
PBN-AR
Instytucja
Instytut Chemii Organicznej Polskiej Akademii Nauk
Informacje podstawowe
Główny język publikacji
en
Czasopismo
EUROPEAN JOURNAL OF ORGANIC CHEMISTRY
ISSN
1434-193X
EISSN
1099-0690
Wydawca
WILEY-BLACKWELL
DOI
URL
Rok publikacji
2013
Numer zeszytu
35
Strony od-do
7867-7871
Numer tomu
2013
Identyfikator DOI
Liczba arkuszy
Streszczenia
Język
angielski
Treść
Adenanthin has been recently shown to inhibit the enzymatic activities of peroxiredoxins (Prdx) I and II through its functional α,β-unsaturated ketone group serving as a Michael acceptor. A similar group is found in SK053, a compound recently developed by our group to target the thioredoxin–thioredoxin reductase (Trx–TrxR) system. This work provides evidence that next to Prdx I and II adenanthin targets additional proteins including thioredoxin–thioredoxin reductase system as well as protein disulfide isomerase (PDI) that contain a characteristic structural motif, referred to as a thioredoxin fold. Adenanthin inhibits the activity of Trx-TR system and PDI in vitro in the insulin reduction assay and decreases the activity of Trx in cultured cells. Moreover, we identified Trx-1 as an adenanthin binding protein in cells incubated with biotinylated adenanthin as an affinity probe. The results of our studies indicate that adenanthin is a mechanism-selective, rather than an enzyme-specific inhibitor of enzymes containing readily accessible, nucleophilic cysteines. This observation might be of importance in considering potential therapeutic applications of adenanthin to include a range of diseases, where aberrant activity of Prdx, Trx–TrxR and PDI is involved in their pathogenesis.
Cechy publikacji
ORIGINAL_ARTICLE
Inne
System-identifier
503356
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