112383-14-9Relevant academic research and scientific papers
Novel azapeptide inhibitors of hepatitis C virus serine protease
Bailey, Murray D.,Halmos, Ted,Goudreau, Nathalie,Lescop, Ewen,Llinàs-Brunet, Montse
, p. 3788 - 3799 (2007/10/03)
Azapeptides are known inhibitors of several serine and cysteine proteases. In seeking different classes of inhibitors for the HCV serine protease, a series of novel azapeptide-based inhibitors were investigated which incorporated noncleavable P1/P1′ aza-a
INHIBITORS OF HUMAN LEUCOCYTE ELASTASE. PEPTIDES INCORPORATING AN &α-AZANORVALINE RESIDUE OR A THIOMETHYLENE LINKAGE IN PLACE OF A PEPTIDE BOND
Dutta, Anand S.,Giles, Michael, B.,Gormley, James J.,Williams, Joseph C.,Kusner, Edward J.
, p. 111 - 120 (2007/10/02)
Peptides containing an α-azanorvaline residue at the C-terminus and N- group at the N-terminus have been made as inhibitors of human leucocyte elastase.A number of analogues with an amide bond replaced by a thiomethylene group have also been prepared.The analogues were tested against leucocyte elastase using MeO-Suc-Ala-Ala-Pro-Val-p-nitroanilide as a substrate and the results were obtained as IC50 values.Both types of analogues inhibited the leucocyte elastase; the most potent of these was N--L-valyl-L-prolyl-α-azanorvaline phenyl ester ( 2 ) ( IC50 0.28 μM, Ki 0.02 μM ).
