ETH Zurich Develops Boron-Based Method to Enhance Protein Synthesis for Cancer Therapies
ETH Zurich researchers have created a new peptide ligation technique utilizing boron chemistry, enabling efficient protein synthesis, especially for aggregation-prone proteins. This method allows assembly at low concentrations, integrating with existing laboratory practices, and could enhance the development of targeted cancer therapies and immunotherapies. Notably, it aids in producing proteins like PD-L2, crucial for immune checkpoint pathways, and may improve antibody-drug conjugates.
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Scientists at ETH Zurich have developed a new peptide ligation method utilizing boron-containing molecules to simplify the synthesis of complex proteins for cancer therapies. This technique operates at micromolar concentrations, allowing for the assembly of proteins that typically aggregate, such as PD-L2, a target in immunotherapy.
The method incorporates a potassium acyltrifluoroborate (KAT) group and a hydroxylamine group for efficient bonding. Additionally, a protecting-group system was designed to integrate this new chemistry with standard peptide synthesis workflows. The advancement could enhance the production of therapeutic proteins and antibody-drug conjugates in modern medicine.
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