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Revolutionary therapy: How new peptides could stop tumor growth!
The University of Bonn is conducting research into the inactivation of cathepsin B, a protease that plays a key role in cancer biology.
Revolutionary therapy: How new peptides could stop tumor growth!
On May 28, 2025, researchers at the University of Bonn about groundbreaking advances in cancer research, particularly with regard to the role of proteases. A recent study shows that the inactivation of an enzyme is possible through targeted interactions between the peptide substrate and the protease. These findings could make a crucial contribution to developing new therapeutic approaches to inhibit tumor progression.
The focus of the research is cathepsin B, a cysteine protease that is upregulated in numerous cancers. This group of enzymes is known to form covalent bonds during peptide bond cleavage. The “right” part of the substrate is released first, while the “left” part remains on the enzyme for a short time. The scientists have set themselves the goal of developing an artificial peptide that occupies these “right” binding pockets and thus inhibits the protease.
Mechanisms of protease inhibition
The study shows that 91 different end products were synthesized and biochemically tested. The mechanism of inactivation was supported by X-ray crystal structure analyzes of enzyme-inhibitor complexes. Cathepsin B plays a central role in malignant progression by promoting tumor growth, angiogenesis, invasion and metastasis in various experimental models. Data shows extremely high levels of cathepsin B in various cancers, including breast, prostate and glioblastoma.
This is supported by further research conducted on the National Institutes of Health was published. There, the causality of cathepsin B in cancer initiation and progression is highlighted. In particular, the absence of cathepsin B in transgenic models was found to be associated with increased rates of apoptosis, indicating its dual role in tumor biology involving both pro-apoptotic and anti-apoptotic effects.
Therapeutic implications and future research
The results so far highlight cathepsin B as a potential therapeutic target in cancer treatment. Studies show that downregulation of this protease can reduce tumor motility and invasion. The discovery of various promoters for the cathepsin B gene and their regulatory mechanisms provides information about the biological functions of these enzymes in tumor development. These findings could lay the foundation for innovative therapeutic strategies.
The challenges in the targeted inhibition of cathepsin B and other proteases are complex. Research has shown that cathepsin B can be compensated for by other cysteine proteases, highlighting the need for multifactorial treatment approaches. An acidic microenvironment around tumors also promotes cathepsin B activity, further adding complexity to the development of targeted therapies.
Finally, in further analysis, the research postulates that disruptive proteases contribute to cancer development by influencing key mechanisms such as ECM remodeling and immune responses. These preliminary results, rounded off by data from the National Institutes of Health, confirm the need to better understand the functions of cathepsin B and other proteases in cancer biology to develop new diagnostic tools and therapeutic options.