Peptide Engineering: From Fluorescent Biomarkers to Bioorthogonal Catalysts

Abstract

Fluorescent proteins have become essential tools for bioimaging, but recent discoveries suggest that peptides lacking aromatic residues can also exhibit fluorescence. This phenomenon, termed clusteroluminescence, arises from the spatial confinement of electron-rich functional groups, leading to electronic delocalization and the formation of emissive clusters. Understanding this mechanism can open new possibilities for non-aromatic fluorescent peptides as bioimaging tools. This project focuses on single alpha-helical peptides (SAHs), particularly the E-R/K alpha-helical motif, which consists of repeating anionic (Glu) and cationic (Lys/Arg) residues that stabilize the structure through salt bridges.