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.
The team’s findings were recently published in the peer-reviewed German scientific journal, Angewandte Chemie. Among the peptides identified, 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 revealed that D’20 effectively blocks MMP7 activity with a high level of accuracy, without affecting other enzymes in the matrix metalloproteinase family.
Notably, the peptide also inhibited the movement of pancreatic cancer cells, a crucial step in preventing the spread of the disease, while allowing normal cell growth to continue.
The stability of D’20 was another remarkable feature highlighted in the study. 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 position it as a promising candidate for future cancer therapies. By effectively targeting MMP7, the peptide could pave the way for more precise treatments for cancers that are currently difficult to treat while reducing side effects.
If further research confirms the effectiveness of D’20 in human trials, the MI-RaPID technology would open new avenues for the development of other highly specific peptide-based treatments.
(Inputs from ANI/TPS)
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