Research offers new hope in fight against pancreatic cancer

21 October,2024 09:08 AM IST |  Jerusalem  |  Agencies

Major breakthrough in targeting the enzyme that facilitates invasion of cancer cells into surrounding tissues

The findings offer new hope to those battling aggressive forms of cancer, particularly in the pancreas. Representation pic


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In a major step forward for cancer treatment, Israeli and Japanese researchers have created a highly targeted inhibitor for an enzyme that plays a critical role in helping cancer grow and spread. The findings offer new hope to patients battling aggressive forms of cancer, particularly in the pancreas.

The research, a collaborative effort involving the Hebrew University of Jerusalem, the Weizmann Institute of Science, and the University of Tokyo, represents a major breakthrough in targeting an enzyme called Matrix Metallopeptidase 7 (MMP7) which facilitates the invasion of cancer cells into surrounding tissues.

MMP7 has structural similarities to other enzymes, which has made developing a drug to specifically block MMP7 without disrupting other essential enzymes a longstanding challenge. But a newly discovered peptide, named D'20, has shown remarkable potential in specifically targeting MMP7 while leaving other similar enzymes untouched.

Peptides are short chains of amino acids that can influence many biological processes and are used in medicine to treat conditions like cancer, diabetes, and autoimmune diseases. D'20's precision could lead to more effective and personalised cancer treatments.

The study, 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, utilised a cutting-edge approach called Mirror-Image Random Nonstandard Peptide Integrated Discovery (MI-RaPID). This advanced peptide discovery technology enabled the researchers to identify a new class of molecule - macrocyclic peptides - that can precisely bind to MMP7, thereby inhibiting its activity.

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