PhD defence Jay Hanssens

Keywords: Peptides, Passerini reaction, Multicomponent Chemistry, C-terminus

"Diving Beyond Protection: Aqueous Passerini Functionalization of Unprotected Peptide C-Termini"

Peptides are small chains of amino acids that play important roles in biology and are increasingly used in medicines and other biomedical applications. Their properties can often be improved by attaching specific chemical groups to them, but making these modifications at exactly the desired position remains challenging. This thesis focuses on developing new ways to selectively modify one particular end of a peptide, known as the C-terminus.

The research uses a chemical reaction called the Passerini reaction to introduce new functionalities onto unprotected peptides under mild, water-based conditions. By combining this reaction with either enzymes or a second chemical ligation method, the researchers developed new approaches for selectively modifying and joining peptides. They also designed new water-soluble chemical building blocks that help prevent modified peptides from becoming insoluble in water. Together, these methods provide new and versatile tools for precisely tailoring peptides, with potential applications in drug development, chemical biology, and the design of new biomaterials.

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