Energy and entropy effects in dissociation of peptide radical anions

Time- and collision energy-resolved surface-induced dissociation (SID) of peptide radical anions was studied using a Fourier transform ion cyclotron resonance mass spectrometer (FT-ICR MS) configured for SID experiments. Peptide radical cations and anions were produced by gas-phase fragmentation of CoIII(salen)-peptide complexes. The effect of the charge, radical, and the presence of a basic residue on the energetics and dynamics of dissociation of peptide ions was examined using RVYIHPF (1) and HVYIHPF (2) as model systems. Comparison of the survival curves of [M+H]+, [M−H]−, M+, and [M−2H]− ions of these precursors demonstrated that even-electron ions are more stable toward fragmentation than their odd-electron counterparts. RRKM modeling of the experimental data demonstrated that the lower stability of the positive radicals is mainly attributed to lower dissociation thresholds while entropy effects are responsible the relative instability of the negative radicals. Substitution of arginine with less basic histidine residue has a strong destabilizing effect on the [M+H]+ ions and a measurable stabilizing effect on the odd-electron ions. Lower threshold energies for dissociation of both positive and negative radicals of 1 are attributed to the presence of lower-energy dissociation pathways that are most likely promoted by the presence of arginine.

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► We studied the effect of the charge, radical, and basic residue on the energetics and dynamics of dissociation of peptide ions.
► We used surface-induced dissociation combined with RRKM modeling.
► Even-electron ions are more stable toward fragmentation than their odd-electron counterparts.
► Fragmentation of radical anions is entropically favored.
► Single population of structures adequately describes the observed kinetics of fragmentation.