Electronic properties of charge-tagged peptides upon electron capture.

We report a computational study of Ala-Lys (AK) and Lys-Ala (KA) dipeptide ions furnished with fixed-charged pyridinium groups that were attached by amide linkers to the N-terminal amino groups. Cation-radicals from one-electron reduction of the doubly charged AK and KA peptide conjugates showed various extents of unpaired electron density being delocalized between the pyridine and peptide moieties. The delocalization depended on the local recombination energies (RE(loc)) of the charged groups. The RE(loc) of the pyridine moieties were modified by introducing electron-donating substituents (CH(3), OCH(3), and N(CH(3))(2)). The RE(loc) of the peptide moieties were found to depend on the peptide conformation and internal solvation of the Lys ammonium groups. Substantial electron delocalization was found for combinations of pyridine substituents and peptide conformers with closely matched RE(loc), such as 4-dimethylamino-pyridine and internally solvated Lys ammonium or unsubstituted pyridine and free (unsolvated) Lys ammonium. The dissociation (DeltaH(diss)) and transition state energies (E(TS)) for the loss of the pyridine ring from the conjugates were found to be DeltaH(diss) = 34-36 kJ mol(-1) and E(TS) = 67-69 kJ mol(-1) for the unsubstituted pyridine moieties, but did not depend much on the peptide sequence.