5504-50-7Relevant articles and documents
Oxidative Dehydrogenative [3+3] Annulation of Benzylhydrazines with Aziridines Leading to Tetrahydrotriazines
Li, Haitao,Liang, Jia,Huo, Congde
supporting information, p. 878 - 882 (2019/07/18)
Oxidative dehydrogenative [3+3] annulation of benzylhydrazines with N-sulfonylaziridines is described. A series of complex tetrahydro-1,2,4-triazines were produced under mild reaction conditions.
Gold-catalyzed three-component spirocyclization: A one-pot approach to functionalized pyrazolidines
Wagner, Bernd,Hiller, Wolf,Ohno, Hiroaki,Krause, Norbert
, p. 1579 - 1583 (2016/02/10)
An efficient, highly atom economic synthesis of hitherto unknown spirocyclic pyrazolidines in a one-pot process was developed. The gold-catalyzed three-component coupling of alkynols, hydrazines and aldehydes or ketones likely proceeds via cycloisomerization of the alkynol to an exocyclic enol ether and subsequent [3 + 2]-cycloaddition of an azomethine ylide. A library of 29 derivatives with a wide range of functional groups was synthesized in up to 97% yield. With this new method, every position in the final product can be substituted which renders the method ideal for applications in combinatorial or medicinal chemistry.
Peptidyl and azapeptidyl methylketones as substrate analog inhibitors of papin and cathepsin B
Calabretta, R.,Giordano, C.,Gallina, C.,Morea, V.,Consalvi, V.,Scandurra, R.
, p. 931 - 942 (2007/10/03)
Peptidyl methylketones containing Phe, Tyr, Tyr(I), Tyr(I2), Leu and Ile in P2 were synthesized and tested as substrate analog revesible of papain and bovine spleen cathepsin B.The most effective cathepsin B inhibitor contained Tyr(I2) and displayed an inhibition constant of 4.7 μM at pH 6.8 and 25 deg C, while Leu or Ile gave practically inert analogs.Replacement of the amino acids in P2 with the analogues α-azaamino acids, as well as the glycine in P1 with α-azaglycine, led to complete loss of inhibiting activity.Introducing alkoxy substituents at themethyl adjacent to the ketone group generally resulted in more effective inhibitors, with inhibition constants in the micromolar range for both papin and cathepsin B. - Keywords: enzyme inhibiting activity; cysteine proptease; slow binding; peptidyl methylketone; azapeptidyl methylketone; papain; cathepsin B