Sulfur-aromatic interactions in peptides: revealing fingerprints in dissociation and structure
Biomolecules such as peptides and proteins adopt complex three-dimensional structures that are essential for their biological function. These structures are formed and stabilized by non-covalent interactions, among which interactions involving sulfur-containing residues such as methionine and aromatic amino acids play a particularly important role. The sulfur–aromatic interaction has been repeatedly identified in protein structures. Its biological significance is underscored by its involvement in pathological processes, including neurodegenerative diseases such as Alzheimer’s and Creutzfeldt–Jakob.
The investigation of biomolecules in the gas phase is an established approach that enables the isolation of intrinsic molecular properties. In combination with mass spectrometry, both collision- and photon-induced techniques are employed to probe structural properties on the molecular level.Building on this framework, in her thesis, Laura Pille investigated the sulfur–aromatic interaction with photon-based action spectroscopy across a broad range of photon energies. She used a series of systematically designed model systems, ranging from small neutral complexes to peptides of increasing size, to disentangle the contributions of aromatic residue type, molecular size, and local chemical environment.