429676-93-7 Usage
Description
Cathepsin G inhibitor I is a potent and selective inhibitor of cathepsin G (IC50 = 53 nM). It weakly inhibits or has no effect on related proteases, including chymotrypsin, thrombin, plasmin, trypsin, tryptase, and elastase.
Uses
Used in Pharmaceutical Industry:
Cathepsin G inhibitor I is used as a therapeutic agent for targeting cathepsin G, which plays a role in various diseases and conditions. Its selective inhibition can help in the development of treatments for conditions where cathepsin G activity is a contributing factor.
Used in Research Applications:
Cathepsin G inhibitor I is used as a research tool for studying the role of cathepsin G in biological processes and disease mechanisms. Its potent and selective inhibition allows researchers to investigate the specific functions and interactions of cathepsin G in cellular and molecular contexts.
Used in Drug Development:
Cathepsin G inhibitor I is used as a lead compound in the development of new drugs targeting cathepsin G. Its potent inhibition of the enzyme can serve as a starting point for designing and optimizing more effective and selective inhibitors for therapeutic use.
references
[1] greco mn, hawkins mj, powell et, almond hr jr, corcoran tw, de garavilla l, kauffman ja, recacha r, chattopadhyay d, andrade-gordon p, maryanoff be. nonpeptide inhibitors of cathepsin g: optimization of a novel beta-ketophosphonic acid lead by structure-based drug design. j am chem soc. 2002;124(15):3810-1.
Check Digit Verification of cas no
The CAS Registry Mumber 429676-93-7 includes 9 digits separated into 3 groups by hyphens. The first part of the number,starting from the left, has 6 digits, 4,2,9,6,7 and 6 respectively; the second part has 2 digits, 9 and 3 respectively.
Calculate Digit Verification of CAS Registry Number 429676-93:
(8*4)+(7*2)+(6*9)+(5*6)+(4*7)+(3*6)+(2*9)+(1*3)=197
197 % 10 = 7
So 429676-93-7 is a valid CAS Registry Number.
429676-93-7Relevant articles and documents
Nonpeptide inhibitors of cathepsin G: Optimization of a novel β-ketophosphonic acid lead by structure-based drug design
Greco, Michael N.,Hawkins, Michael J.,Powell, Eugene T.,Almond Jr., Harold R.,Corcoran, Thomas W.,De Garavilla, Lawrence,Kauffman, Jack A.,Recacha, Rosario,Chattopadhyay, Debashish,Andrade-Gordon, Patricia,Maryanoff, Bruce E.
, p. 3810 - 3811 (2007/10/03)
The serine protease cathepsin G (EC 3.4.21.20; Cat G), which is stored in the azurophilic granules of neutrophils (polymorphonuclear leukocytes) and released on degranulation, has been implicated in various pathological conditions associated with inflammation. By employing high-throughput screening, we identified β-ketophosphonic acid 1 as a moderate inhibitor of Cat G (IC50 = 4.1 μM). We were fortunate to obtain a cocrystal of 1 with Cat G and solve its structure by X-ray crystallography (3.5 A). Structural details from the X-ray analysis of 1·Cat G served as a platform for optimization of this lead compound by structure-based drug design. With the aid of molecular modeling, substituents were attached to the 3-position of the 2-naphthyl ring of 1, which occupies the S1 pocket of Cat G, to provide an extension into the hydrophobic S3 region. Thus, we arrived at analogue 7 with an 80-fold potency improvement over 1 (IC50 = 53 nM). From these results, it is evident that the β-ketophosphonic acid unit can form the basis for a novel class of serine protease inhibitors. Copyright
