Electron transfer ion/ion reactions in a three-dimensional quadrupole ion trap: reactions of doubly and triply protonated peptides with SO2*-

Abstract

Ion-ion reactions between a variety of peptide cations (doubly and triply charged) and SO2 anions have been studied in a 3-D quadrupole ion trap, resulting in proton and electron transfer. Electron transfer dissociation (ETD) gives many c- and z-type fragments, resulting in extensive sequence coverage in the case of triply protonated peptides with SO2*-. For triply charged neurotensin, in which a direct comparison can be made between 3-D and linear ion trap results, abundances of ETD fragments relative to one another appear to be similar. Reactions of doubly protonated peptides with SO2*- give much less structural information from ETD than triply protonated peptides. Collision-induced dissociation (CID) of singly charged ions formed in reactions with SO2*- shows a combination of proton and electron transfer products. CID of the singly charged species gives more structural information than ETD of the doubly protonated peptide, but not as much information as ETD of the triply protonated peptide.

Figure 1

(a) Product spectrum from the reaction of RKRARKE [M + 3H]³⁺ with SO₂^·−. b) Product spectrum from reaction of RKRARKE [M + 2H]²⁺ with SO₂^·−.

Figure 2

(a) Product spectrum from the reaction of guanidinated KGAILKGAILR [M + 3H]³⁺ with SO₂^·−. (b) Product spectrum from the reaction of guanidinated KGAILKGAILR [M + 2H]²⁺ with SO₂^·−. K represents homoarginine.

Figure 3

(a) Product spectrum from the reaction of neurotensin [M + 2H]²⁺ with SO₂^·−. (b) CID of the singly charged peptide species from (a).

Scheme 1

Standard Fragmentation Nomenclature for Peptides,