Selectivity in ROS-induced peptide backbone bond cleavage

Hannah M. Stringfellow, Michael R. Jones, Mandy C. Green, Angela K. Wilson, Joseph S. Francisco

Research output: Contribution to journalArticlepeer-review

15 Scopus citations


Post-translational mechanisms of protein oxidation as a result of reactive oxygen species (ROS) can occur under physiological conditions to yield selective side-chain and backbone modifications including abstractions, donations, additions, substitutions, and fragmentation. In order to characterize the selectivity of radical-mediated fragmentation, quantum mechanical investigations using ab initio and density functional methods were employed to evaluate site, conformation, and pathway trends of small trialanine peptides resembling a β-strand and a β-turn. Comparisons of reaction enthalpies show that the diamide pathway is more energetically favorable than the α-amidation pathway and that both pathways are site and conformationally selective. These findings readily contribute to the understanding of oxidative stress in biochemical processes. (Figure Presented).

Original languageEnglish (US)
Pages (from-to)11399-11404
Number of pages6
JournalJournal of Physical Chemistry A
Issue number48
StatePublished - Dec 4 2014
Externally publishedYes

ASJC Scopus subject areas

  • Physical and Theoretical Chemistry


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