Work

Dimethyl labeling of N-terminal amines allows unambiguous identification of protein crosslinks

Year: 2024

Type: article

Abstract: O-approach including high labeling yields (92-100 %) and well-defined mass spectrometric isotope distribution patterns. This approach has allowed identification of novel dityrosine crosslinks between pair of tyrosine (Tyr, Y) residues in photo-oxidized β-casein (Y195-Y195, Y195-Y208, Y208-Y208), and α-synuclein exposed to nitrosative stress (Y39-Y39, Y39-Y125, Y39-Y133, Y133-Y136). This approach is also applicable to disulfide bond mapping, with 15 of 17 disulfides in serum albumin readily detected. These data indicate that dimethyl labeling is a highly versatile and efficient approach for the site-specific identification of oxidation- and nitration-induced crosslinks in proteins.

Source: Free Radical Biology and Medicine

DOI: 10.1016/j.freeradbiomed.2024.12.002

Authors: Tina Nybo, Luke F. Gamon, Eduardo Fuentes-Lemus, Daniel E. Otzen, Michael J. Davies, Per Hägglund

Institutions: University of Copenhagen, Aarhus University

Language: English

Topic: Redox biology and oxidative stress

Subfield: Molecular Biology

Field: Biochemistry, Genetics and Molecular Biology

Domain: Life Sciences

Open Access status: hybrid

Estimated APC paid: $3,740