UVPD of peptides modified with N-terminal UV-absorbing chromophores

ABSTRACT: Ultraviolet photodissociation (UVPD) has emerged as a powerful alternative to conventional collision-induced dissociation (CID) for peptide and protein sequencing in mass spectrometry–based proteomics. However, UVPD efficiency depends on the presence of UV-absorbing chromophores within analytes.The uploaded dataset is a systematic investigation of how N-terminal modification of peptides with aromatic chromophores influences 193 nm UVPD efficiency and fragmentation behavior. Using NHS ester chemistry, human cell lysate digests were derivatized with a range of UV-absorbing aromatic labels and analyzed on an Omnitrap–Orbitrap platform equipped with a 193 nm ArF excimer laser. Compared with unmodified controls, derivatized peptides displayed modestly increased fragmentation efficiency and greater diversity of sequence-informative fragments, particularly b-type ions. Peptides lacking aromatic amino acids benefited most from N-terminal aromatic labeling, exhibiting enhanced fragmentation and sequence coverage. These findings demonstrate that incorporation of aromatic chromophores at the N-terminus can enhance UVPD performance and improve spectral interpretability, thereby expanding the applicability of UVPD in bottom-up proteomics workflows.

INSTRUMENT(S):

ORGANISM(S): Homo Sapiens (human)

TISSUE(S): Kidney

SUBMITTER: Nikita Levin  

LAB HEAD: Shabaz Mohammed

PROVIDER: PXD075227 | Pride | 2026-06-08

REPOSITORIES: Pride