ANTI CATHEPSIN B MARKET ANALYSIS

Anti Cathepsin B MarketSize and Trends

The Global Anti-Cathepsin B Market is estimated to be valued at US$ 187.0 Million in 2023 and is expected to exhibit a CAGR of 3.2 % during the forecast period (2023-2030).

Global Anti-Cathepsin B Market: Key Trends

Introduction of new research in anti-cathepsin B

The introduction of new research in anti-cathepsin B can drive market growth. On April 3, 2023, MDPI, Switzerland-based publisher, explained cathepsin B tends to be overexpressed in many cancer cells, hence its inhibitors may be useful as anticancer medications. It was anticipated that the newly developed self-assembled cathepsin B inhibitor would be able to get around the restrictions that now exist for cytotoxic medicines used in cancer treatment. The hydrophilic peptide sequence of Arg-Arg (RR), which is unique to cathepsin B, was conjugated directly to the hydrophobic ursodeoxycholic acid (BA) in order to create a peptide-based biomolecule that could bind to cathepsin B. Due to ursodeoxycholic acid's safety and US-FDA approval as a medicine, this was able to create a peptide-drug conjugate (PDC). Ethylamide (NHEt) inhibited the carboxylic end of the RR peptide to stop unneeded side effects.

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.