135941-88-7Relevant academic research and scientific papers
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
Sodium cyanoborohydride reduction of (benzyloxycarbonyl)- and (tert-butoxycarbonyl)hydrazones
Calabretta,Gallina,Giordano
, p. 536 - 539 (2007/10/02)
(Benzyloxycarbonyl)- and (tert-butoxycarbonyl)hydrazones are easily reduced by sodium cyanoborohydride in acidic medium. The method is an alternative to catalytic hydrogenation and allows ready access to both N-benzyloxycarbonyl and N-tert-butoxycarbonyl
