Revolutionary study: How artificial peptides can stop cancer proteases!

Revolutionary study: How artificial peptides can stop cancer proteases!

A current study of study at the University of Bonn reveals exciting new insights into the role of proteases, especially Cathepsin B, in connection with cancer. These enzymes show a complex interaction with peptides, which are characterized by covalent bonds during peptide binding split. The study deals with the mechanism of how Cathepsin B is involved in tumor progression and at the same time develops innovative inhibitors to inhibit this protease. With the aim of creating an artificial peptide that occupies the "right" binding bags of Cathepsin B and blocked the enzyme activity, 91 different end products were synthesized and tested biochemically. X -ray crystal structure analyzes provided a solid basis for securing these mechanisms.

Cathepsin B, a cysteine ​​protease, plays a significant role in different phases of malignant tumor development. The studies show that high mirrors of Cathepsin B can be found in numerous human cancer, often associated with the cell membrane of tumor cells. In transgenic models, research has demonstrated a causal role of Cathepsin B in the initiation, growth, angiogenesis, as well as invasion and metastasis. These findings underline the importance of Cathepsin B as a potential therapeutic goal in cancer treatment.

The role of Cathepsin B

Research on the dysregulation of proteases has meaning for cancer biology and therapy -mandatory approaches. Cathepsin B is involved in apoptosis by splitting both pro-apoptotic and anti-apoptotic proteins. Vivo models show that Cathepsin B plays a crucial role during tumor development, whereby the overexpression of these protease is often correlated with more aggressive tumor biology. Furthermore, the local acidic micro environment around tumors can promote the activity of Cathepsin B, which further strengthens its role in tumor progression.

The development of such peptidomimetics that act as inhibitors is an important step in preclinical research. In addition to focusing on Cathepsin B, the potential of other proteases is also examined, which could work through similar mechanisms in cancer progression. Another goal is cell culture models to characterize the biological activity of these inhibitors, which is of crucial importance for the development of future therapeutic agents.

therapeutic approaches and challenges

Research shows that the down -to -regulation of Cathepsin B reduces tumor tomotility and invasion. These findings indicate that a combination of inhibitors could potentially be more effective than therapy that aims exclusively on Cathepsin B. The close association of Cathepsin B with the tumor cell membrane is a challenge. For therapeutic strategies, it is therefore important to understand the mechanisms that lead to increased expression of cathepsin B in tumors, as well as their effect on tumor biology.

This exciting research carried out at the University of Bonn opens up promising prospects in cancer research. It emphasizes the need to develop innovative therapeutic approaches and to better understand the complex interactions of proteases in the tumor mouge field. The aim is to develop more effective treatment strategies in the future that aim at the specific biological mechanisms of cancer.

For more information about the results of the study, please visit the website of the University Bonn , the article on Pubmed Central , as well as the contribution on dysregulated proteases on pubmed central .