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Peptides developed by Michigan researchers could lead to a targeted therapy for half of all prostate cancer patients. University of Michigan researchers have identified a large molecule that selectively attacks prostate tumors that have a genetic anomaly without harming healthy cells. This mutation affects half of all prostate cancer patients. The fusion of the genes TMPRSS2 and ERG is a key step in the development of prostate cancer, but it has been difficult to target with small-molecule drugs. Gene rearrangements are deemed poor drug targets because of their location within the cell’s nucleus and absence of enzyme activity. The Michigan team tested large-molecule peptides in animal models, finding that it disrupted ERG function and curbed the growth of prostate tumors that expressed the gene fusion. The peptides did not affect cells without ERG fusion. The research is published in Cancer Cell. “This is an example of how we can deliver precision therapy for prostate cancer: Only patients who have the ERG gene fusion would be matched with this agent. But it’s useful because the ERG fusion is so prevalent,” said senior author Arul Chinnaiyan, M.D., director of the Michigan Center for Translational Pathology and a professor of pathology at Michigan. After skin cancer, prostate cancer is the most common cancer and the third-leading cause of cancer death in American men, according to the American Cancer Society.The five-year survival rate for local- and regional-stage prostate cancer is nearly 100%, but it drops dramatically to 28% for prostate cancer that has spread to distant lymph nodes, bones or other organs. But some men appear to have treatable, localized cancer, yet end up developing aggressive metastasis. University of Toronto scientists pinpointed a set of genetic mutations that could help oncologists predict a patient’s risk of their cancer spreading after treatment. Meanwhile, Tokai, which has been working on the small molecule galeterone, hit a snag last summer when the drug failed in a phase 3 trial. The company laid off more than half its staff and stopped enrollment of a galeterone trial in patients with metastatic castration-resistant prostate cancer who have become resistant to the drug Xtandi. While the large-molecule approach is promising, it has a couple of hurdles to overcome. The peptides tend to break down quickly, before they arrive at the target, while large molecules can’t pass through the cell membrane. The University of Michigan researchers sidestepped the first issue by creating protein-like chains that were mirror images of the peptides. The team plans to create a 3D outline of how the peptides bind to ERG, with the goal of developing a small molecule that blocks ERG. WarningTHE GOODS OFFERED BY THE SELLER IS INTENDED FOR SCIENTIFIC AND DEVELOPMENT PURPOSES ONLY. The goods offered by the Seller include chemical substances that shall not be used as a drug, medicine, active substance, medical aid, cosmetic product, a substance for production of a cosmetic product neither for human consumption that is any food or food supplement or otherwise similarly used on humans or animals. References / Links Rahim, S., Minas, T., Hong, S. H., Justvig, S., Celik, H., Kont, Y. S., Han, J., Chen, K., Li, Y., Kong, Y., Ma, Y., Sun, Y., Triche, T., Bieging-Rolett, K., Tuntland, T., Serkova, N., Ratan, R., O’Hare, P., & Chinnaiyan, A. M. (2014). A small molecule inhibitor of ERG for prostate cancer treatment. Cancer Cell, 26(2), 151–165. PubMed Shaikhibrahim, Z., Offermann, A., Braun, M., Menon, R., Queisser, A., Boehm, D., Nowak, M., Perner, S., & Kristiansen, G. (2012). ERG fusion protein expression and serine 21 phosphorylation in prostate cancer. The Prostate, 72(11), 1213–1221. PubMed Tomlins, S. A., Rhodes, D. R., Perner, S., Dhanasekaran, S. M., Mehra, R., Sun, X. W., Varambally, S., Cao, X., Tchinda, J., Kuefer, R., Lee, C., Montie, J. E., Shah, R. B., Pienta, K. J., Rubin, M. A., & Chinnaiyan, A. M. (2005). Recurrent fusion of TMPRSS2 and ETS transcription factor genes in prostate cancer. Science, 310(5748), 644–648. PubMed Nguyen, H. G., & Yang, C. S. (2021). Targeting TMPRSS2-ERG fusion in prostate cancer: therapeutic implications. Frontiers in Oncology, 11, 679826. PubMed

First of all, it is necessary to highlight the fact that more than 7000 naturally occurring peptides have been gradually discovered since the last century. In the human body, these peptides perform many important roles as hormones, growth factors, neurotransmitters, ion channel ligands or anti-infective agents. Research peptides are simply those that are used in scientific research for the purpose of obtaining knowledge and the results of their action, especially for the development of future farmaceuticals. Interest in peptides has increased recently, especially from pharmaceutical research and development. These potent and selective signaling molecules, which bind to specific cell surface receptors in the body to trigger various intracellular effects, have been shown to be highly effective and relatively safe in therapeutic applications. They are generally very well tolerated by patients and participants in clinical trials. Their action is highly selective and effective, therefore this promising potential in the field of medical use is the driving force for new and new research, studies and experiments. The surge in demand for research peptides is therefore part of the path to the pharmaceuticals and therapeutics of the future and overall progress in the field. Research Peptides vs Medicines? The essential difference between approved medicines and research peptides is that research peptides are intended exclusively for scientific and research purposes and experiments "in vitro", which means "in glass", that is, outside the body. They are not yet approved as medicines that a doctor could prescribe to treat any disease. Hundreds of peptide therapeutics have already been investigated and evaluated in clinical trials. It is the research that many scientists around the world are doing that often uses research peptides in laboratories to study beyond traditional peptide design. The goal is to discover variants of peptides that could subsequently become pharmaceuticals. On the basis of peptides, about 60 pharmaceutical medicines have already reached the market, which have passed everything necessary for approval by the authorities. In the US, it is the Food and Drug Administration (FDA) that must approve the medicine. Examples include the prostate cancer treatment LupronTM or the type 2 diabetes treatment VictozaTM. Both of these medicines achieved large sales turnovers. Such approved drugs are not research peptides. Research peptides cannot be listed or prescribed as medicines. Although they show excellent and safe results and effects in studies, they must go through a rigorous process of clinical trials and subsequent FDA approval. They can be used for research and scientific purposes, as they could lead to very important new discoveries and the development of future drugs. However, until then, they cannot be prescribed or used for prevention by doctors. Research Peptides As a Basis For Future Medicines Due to the promising potential of peptides for medical applications, more and more intensive research, studies and experiments with peptides are needed in order to discover the pharmaceutical substances of the present and future. Therefore, the demand for research peptides is increasing intensively to support the progress in these new fields of research. In clinical studies, research peptides have demonstrated exceptional safety and tolerability by study participants, while maintaining high selectivity, efficacy, and predictable metabolism. Peptides therefore represent a huge opportunity for further therapeutic development. The large increase in obesity and type 2 diabetes, as well as cancer mortality, has made these two areas one of the main areas that drive research and development of peptide-based medicines. In North America, but not only there, metabolic diseases such as obesity and diabetes are a serious and growing problem. Similarly, the increase in deaths from oncological diseases leads to the search for alternatives to traditional chemotherapy. Both of these areas call for the development of peptide-based medicines and stimulate further research. However, peptide research has also expanded into other areas. For example, in the field of infectious diseases, inflammation or rare diseases, and it could also have potential in diagnosis and vaccination. Thus, research peptides serve as the basis for experiments and development in laboratories. Crucial research and studies take place there, focusing mainly on uncovering and proving the therapeutic potential of peptides for future medicines. They are therefore extremely important for the further development and possible effective future medicines that could be used in the treatment of serious diseases. WarningTHE GOODS OFFERED BY THE SELLER IS INTENDED FOR SCIENTIFIC AND DEVELOPMENT PURPOSES ONLY. The goods offered by the Seller include chemical substances that shall not be used as a drug, medicine, active substance, medical aid, cosmetic product, a substance for production of a cosmetic product neither for human consumption that is any food or food supplement or otherwise similarly used on humans or animals. References / Links Fosgerau, K., & Hoffmann, T. (2015). Peptide therapeutics: current status and future directions. Drug Discovery Today, 20(1), 122–128.DOI Otvos, L., & Wade, J. D. (2014). Current challenges in peptide-based drug discovery. Frontiers in Chemistry, 2, 62.DOI Muttenthaler, M., King, G. F., Adams, D. J., & Alewood, P. F. (2021). Trends in peptide drug discovery.Nature Reviews Drug Discovery, 20, 309–325. DOI Lau, J. L., & Dunn, M. K. (2018). Therapeutic peptides: Historical perspectives, current development trends, and future directions. Bioorganic & Medicinal Chemistry, 26(10), 2700–2707.DOI FDA – Drugs@FDA Database - https://www.accessdata.fda.gov/scripts/cder/daf/ Craik, D. J., Fairlie, D. P., Liras, S., & Price, D. (2013).The future of peptide-based drugs. Chemical Biology & Drug Design, 81(1), 136–147. DOI