81391-71-1Relevant academic research and scientific papers
Azadipeptide nitriles: Highly potent and proteolytically stable inhibitors of papain-like cysteine proteases
Loeser, Reik,Frizler, Maxim,Schilling, Klaus,Guetschow, Michael
supporting information; experimental part, p. 4331 - 4334 (2009/02/08)
(Chemical Presented) Nitrogen instead of carbon: Azadipeptide nitriles resulting from CH/N exchange in the P1 position (see picture) are hitherto unknown. To access these compounds by conversion of amino acid-derived hydrazides with cyanogen bromide both nitrogen atoms of the hydrazide must be substituted. Despite a methylated P2-P1 peptide bond, the azadipeptide nitriles show a strong inhibitory activity against cysteine proteases, and a high stability towards chymotryptic hydrolysis.
1-peptidyl-2-haloacetyl hydrazines as active site directed inhibitors of papain and cathepsin B
Giordano,Calabretta,Gallina,Consalvi,Scandurra
, p. 1497 - 1516 (2007/10/02)
Fifteen 1-peptidyl-2-haloacetyl hydrazines, which can be considered halometanes of azapeptides containing Phe in P2 and α-aza-Ala or α-aza-Gly in P1, were synthesized and tested as models of cysteine-proteases inhibitors. By use of k
