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Chiral Molecules Pave the Way for Improved Cancer Therapies

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Researchers from Scripps Research Institute have developed an innovative technique to identify small molecules that can alter protein functions, enhancing targeted drug discovery efforts. The method, described in the journal Molecular Cell, utilizes mirror-image versions of small molecules to detect their impact on cancer-related proteins, moving beyond previous approaches that only assessed binding without functional effects. By analyzing how these molecules influence the size of protein complexes within cells, the researchers identified specific compounds capable of modifying protein functions.

Led by Benjamin Cravatt, the team found a molecule called MY-1B that disrupts the PA28 protein complex linked to protein degradation in cancer. This breakthrough offers groundbreaking tools for exploring protein behavior and potential therapeutic applications. Another compound, EV-96, was found to affect a protein complex involved in RNA splicing, leading to reduced cancer cell growth.

The study underscores the importance of differentiating between mere protein interaction and functional impact, allowing researchers to better target proteins of interest. The team aspires to expand this approach for studying various cell types and exploring additional biological effects, enhancing drug discovery capabilities with these novel chemical tools.

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