Synthesis and Biological Evaluation of Papain-Family Cathepsin L-Like Cysteine Protease Inhibitors Containing a 1,4-Benzodiazepine Scaffold as Antiprotozoal Agents

ChemMedChem ◽  
2014 ◽  
pp. n/a-n/a ◽  
Author(s):  
Roberta Ettari ◽  
Andrea Pinto ◽  
Lucia Tamborini ◽  
Ilenia C. Angelo ◽  
Silvana Grasso ◽  
...  
Keyword(s):  
Protease Inhibitors ◽  
Cysteine Protease ◽  
Cathepsin L ◽  
Biological Evaluation ◽  
Cysteine Protease Inhibitors ◽  
Synthesis And Biological Evaluation

scholarly journals Studies of Inhibitory Mechanisms of Propeptide-Like Cysteine Protease Inhibitors

2014 ◽  
Vol 2014 ◽  
pp. 1-10 ◽  
Author(s):  
Bui T. T. Nga ◽  
Yuki Takeshita ◽  
Misa Yamamoto ◽  
Yoshimi Yamamoto
Keyword(s):  
Protease Inhibitors ◽  
Cysteine Protease ◽  
Cathepsin L ◽  
Cysteine Residue ◽  
Cysteine Protease Inhibitor ◽  
Inhibition Mechanism ◽  
Cysteine Protease Inhibitors ◽  
Inhibitory Potency ◽  
Inhibitory Mechanisms

Mouse cytotoxic T-lymphocyte antigen-2α (CTLA-2α), Drosophila CTLA-2-like protein (crammer), and Bombyx cysteine protease inhibitor (BCPI) belong to a novel family of cysteine protease inhibitors (I29). Their inhibitory mechanisms were studied comparatively. CTLA-2α contains a cysteine residue (C75), which is essential for its inhibitory potency. The CTLA-2α monomer was converted to a disulfide-bonded dimer in vitro and in vivo. The dimer was fully inhibitory, but the monomer, which possessed a free thiol residue, was not. A disulfide-bonded CTLA-2α/cathepsin L complex was isolated, and a cathepsin L subunit with a molecular weight of 24,000 was identified as the interactive enzyme protein. Crammer also contains a cysteine residue (C72). Both dimeric and monomeric forms of crammer were inhibitory. A crammer mutant with Cys72 to alanine (C72A) was fully inhibitory, while the replacement of Gly73 with alanine (G73A) caused a significant loss in inhibitory potency, which suggests a different inhibition mechanism from CTLA-2α. BCPI does not contain cysteine residue. C-terminal region (L77-R80) of BCPI was essential for its inhibitory potency. CTLA-2α was inhibitory in the acidic pH condition but stabilized cathepsin L under neutral pH conditions. The different inhibition mechanisms and functional considerations of these inhibitors are discussed.

scholarly journals Apoferritin encapsulation of cysteine protease inhibitors for cathepsin L inhibition in cancer cells

RSC Advances ◽  
2019 ◽  
Vol 9 (63) ◽  
pp. 36699-36706 ◽  
Author(s):  
José C. Quilles Junior ◽  
Fernanda dos Reis Rocho Carlos ◽  
A. Montanari ◽  
Andrei Leitão ◽  
Viviane W. Mignone ◽  
...  
Keyword(s):  
Cancer Cells ◽  
Protease Inhibitors ◽  
Cysteine Protease ◽  
Cathepsin L ◽  
Cysteine Protease Inhibitors ◽  
Selective Uptake

Novel apoferritin encapsulated cysteine protease inhibitors are developed with enhanced and selective uptake by cancer cells, and sustained pH-induced release of the agent. The persistent inhibition of cathepsin L is demonstrated in vitro.

Evaluation of a microassay for human kininogens as cysteine protease inhibitors

1991 ◽  
Vol 26 (2) ◽  
pp. 113-124 ◽  
Author(s):  
Tove S. Karlsrud ◽  
Ansgar O. Aasen ◽  
Harald T. Johansen
Keyword(s):  
Protease Inhibitors ◽  
Cysteine Protease ◽  
Cysteine Protease Inhibitors

The 1,4-naphthoquinone scaffold in the design of cysteine protease inhibitors

2007 ◽  
Vol 15 (15) ◽  
pp. 5340-5350 ◽  
Author(s):  
Cláudia Valente ◽  
Rui Moreira ◽  
Rita C. Guedes ◽  
Jim Iley ◽  
Mohammed Jaffar ◽  
...  
Keyword(s):  
Protease Inhibitors ◽  
Cysteine Protease ◽  
Cysteine Protease Inhibitors
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