In a significant advancement for cancer treatment, researchers from Israel and Japan have developed a highly targeted inhibitor for an enzyme crucial to cancer growth and spread. This breakthrough offers new hope for patients fighting aggressive cancers, particularly pancreatic cancer. The collaborative research, involving the Hebrew University of Jerusalem, the Weizmann Institute of Science, and the University of Tokyo, focuses on Matrix Metallopeptidase 7 (MMP7), an enzyme that aids cancer cell invasion into surrounding tissues.
MMP7's structural similarities to other enzymes have long posed challenges in creating a drug that specifically targets MMP7 without affecting essential enzymes. However, a newly discovered peptide, named D'20, shows remarkable potential in specifically targeting MMP7 while leaving other similar enzymes unaffected. Peptides, short chains of amino acids, are used in medicine to treat various conditions, including cancer, diabetes, and autoimmune diseases. D'20's precision could lead to more effective and personalized cancer treatments.
Led by Professor Norman Metanis and PhD student Hiba Ghareeb from the Hebrew University, along with Professor Irit Sagi from the Weizmann Institute and Professor Hiroaki Suga from the University of Tokyo, the study employed a cutting-edge approach called Mirror-Image Random Nonstandard Peptide Integrated Discovery (MI-RaPID). This technology enabled the identification of a new class of molecule—macrocyclic peptides—that can precisely bind to MMP7, inhibiting its activity. The team's findings were recently published in the peer-reviewed German scientific journal, Angewandte Chemie.
Among the identified peptides, D'20 stood out for its unique properties. Designed as a mirror-image peptide, D'20 consists of twelve specially modified building blocks known as D-amino acids, which help maintain its stability and specificity. Laboratory tests showed that D'20 effectively blocks MMP7 activity with high accuracy, without affecting other enzymes in the matrix metalloproteinase family. Notably, the peptide also inhibited the movement of pancreatic cancer cells, crucial for preventing disease spread, while allowing normal cell growth to continue.
Another remarkable feature of D'20 is its stability. The peptide retained its structure and function even when exposed to human blood and conditions simulating the digestive system. The researchers believe that D'20's selectivity and stability make it a promising candidate for future cancer therapies. By effectively targeting MMP7, the peptide could lead to more precise treatments for cancers that are currently difficult to treat, while reducing side effects.
If further research confirms D'20's effectiveness in human trials, the MI-RaPID technology could open new avenues for developing other highly specific peptide-based treatments.
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