ANTI CATHEPSIN B MARKET ANALYSIS

Market Challenges And Opportunities

Global Anti-Cathepsin B Market- Drivers

Increasing research in anti cathepsin B market

Increasing research in anti cathepsin B market is expected to drive the global anti-cathepsin b market growth over the forecast period. For instance, on May 5, 2021, OAE Publishing Inc., multidisciplinary publishing company based in the U.S., explained the structure-activity connection of a number of newly developed auranofin derivatives was examined in this in silico investigation with reference to their cathepsin B inhibitory action. A set of well-known cathepsin B inhibitors was used to construct and test a thorough molecular screening model. During the preliminary phase of the biological screening of recently developed inhibitors, its validity was further examined. A series of subsequent in silico predictions of compound inhibitory activity were generated, which led to new structures with increased inhibitory activity and selectivity towards cathepsin B. These predictions were based on the structure-function relationships discovered by recording the empirical score values generated for the screening model.

Global Anti-Cathepsin B Market: Restraints

Complications associated with anti-cathepsin B

Complications associated with anti-cathepsin B can hamper the growth of the market. For instance, John Wiley & Sons, Inc, a publishing company published on January 28, 2020 cathepsin B, a major lysosomal protease, displays both endopeptidase and carboxypeptidase activity. The authors showed that Z-Phe-Arg, Z-Phe-Lys, and Z-Val-Lys dipeptides were used in doxorubicin-based prodrugs, which caused cathepsin B to quickly activate them. However, because arginine and lysine at the P1 position of the protease substrate are excellent targets for a variety of proteases, the authors substituted citrulline (Cit) in place of the Arg/Lys residue. Both prodrugs hydrolyzed equally quickly in rat lysosomal extracts, despite the fact that cathepsin B hydrolyzed the Z-Val-Cit prodrug significantly more slowly than its Z-Val-Lys analog did. This suggested that Val-Cit hydrolysis may involve proteases other than cathepsin B. Therefore, it is crucial to examine the substrate specificity for other proteases that share the same localization and may therefore contribute to unintentional prodrug activation while developing novel peptide linkers.

To counterbalance this restraint, a mechanism of the anti-cathepsin B should be demonstrated in a simple way.