229975-46-6Relevant academic research and scientific papers
Facile synthesis of 1,4-benzodiazepine-2,5-diones and quinazolinones from amino acids as anti-tubercular agents
Anil, Seegehalli M.,Shobith, Rangappa,Kiran, Kuppalli. R.,Swaroop, Toreshettahally R.,Mallesha, Ningegowda,Sadashiva, Maralinganadoddi P.
supporting information, p. 182 - 187 (2019/01/04)
A family of 1,4-benzodiazepine-2,5-diones and quinazolinones with diverse substituents at the C-3 position were synthesized via a novel, simple and convenient methodology using H2PtCl6 as the catalyst. The substitution at the C-3 pos
Chemoenzymatic synthesis of new fluorogenous substrates for cysteine proteases of the papain family
Semashko,Lysogorskaya,Oksenoit,Bacheva,Filippova
, p. 339 - 343 (2008/12/22)
A chemoenzymatic synthesis was developed for new highly specific fluorogenic substrates for cysteine proteases of the papain family, Abz-Phe-Ala-pNA (I) and Glp-Phe-Ala-Amc (II) (Abz, pNA, Glp, and Amc are o-aminobenzoyl, p-nitroanilide, pyroglutamyl, and 4-amino-7-methylcoumaride, respectively). Substrate (I) was obtained in an aqueous-organic medium using native chymotrypsin. Substrate (II) was synthesized in DMF-MeCN by the treatment with chymotrypsin and subtilisin Carlsberg immobilized on polyvinyl alcohol cryogel. Hydrolysis of substrate (I) with papain, ficin, and bromelain was accompanied by a 15-fold increase in fluorescence intensity, and that of substrate (II), by a change in the fluorescence spectrum. Unambiguity of enzymatic hydrolysis of the substrates after the Ala residue was shown. The specific activity of the substrate hydrolysis with papain, bromelain, and ficin and was determined. Papain showed the greatest activity for both substrates. The activity of all proteases under study was essentially higher for substrate (II), than for substrate (I). The lowest detectable papain concentrations were 2.4 × 10-10 M for (I) and 1.2 × 10-11 M for (II). A high selectivity of cysteine proteases for Glp-Phe-Ala-Amc was established.
