Research teams from the Universities of Marburg and Geneva have discovered that the mirror-image amino acid D-cysteine can specifically inhibit the growth of certain cancer cells. The results, published in the journal Nature Metabolism, shed light on the underlying molecular mechanisms and show possible approaches for tumor therapy.

In contrast to the natural amino acid L-cysteine, which is essential for protein synthesis, D-cysteine cannot be used to build protein molecules. The researchers found that D-cysteine acts in tumor cells that have high levels of a specific cysteine transporter in the cell membrane. This transporter, which normally absorbs L-cysteine and thus promotes tumor growth, also enables the uptake of D-cysteine, which, however, triggers toxic effects in the cell.

The Marburg team, led by Prof. Roland Lill, an expert in iron-sulphur proteins, showed that D-cysteine blocks a key enzyme that incorporates sulphur from L-cysteine into iron-sulphur proteins. These proteins are essential for vital processes such as DNA synthesis. The mirror-image structure of D-cysteine prevents sulfur transfer because the sulfur cannot be transferred to the right place in the enzyme. This leads to a lack of functional iron-sulfur proteins, which causes the tumor cells to die.

Initial tests on mice in the Geneva laboratory confirmed that D-cysteine can significantly inhibit tumor growth. The results indicate a high potential for tumor therapy. The researchers now plan to further test the suitability of D-cysteine for clinical use in order to develop new approaches in cancer therapy.

Original Paper:

D-cysteine impairs tumour growth by inhibiting cysteine desulfurase NFS1 | Nature Metabolism

Editor: X-Press Journalistenbüro GbR

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