The effect of the secondary structure on dissociation of peptide radical cations: fragmentation of angiotensin III and its analogues.
Fragmentation of protonated RVYIHPF and RVYIHPF-OMe and the corresponding radical cations was studied using time- and collision energy-resolved surface-induced dissociation (SID) in a Fourier transform ion cyclotron resonance mass spectrometer (FT-ICR MS) specially equipped to perform SID experiments. Peptide radical cations were produced by gas-phase fragmentation of Co (III)(salen)-peptide complexes. Both the energetics and the mechanisms of dissociation of even-electron and odd-electron angiotensin III ions are quite different. Protonated molecules are much more stable toward fragmentation than the corresponding radical cations. RRKM modeling of the experimental data suggests that this stability is largely attributed to differences in threshold energies for dissociation, while activation entropies are very similar. Detailed analysis of the experimental data obtained for radical cations demonstrated the presence of two distinct structures separated by a high free-energy barrier. The two families of structures were ascribed to the canonical and zwitterionic forms of the radical cations produced in our experiments.
Yang
Zhibo
Z
Fundamental Sciences Division, Pacific Northwest National Laboratory, Richland, WA 99352, USA.
Lam
Corey
C
Chu
Ivan K
IK
Laskin
Julia
J
D000595:Amino Acid Sequence; D000805:Angiotensin III / Q000031:analogs & derivatives* / Q000737:chemistry* / Q000378:metabolism; D003035:Cobalt / Q000378:metabolism; D003300:Copper / Q000378:metabolism; D005583:Fourier Analysis; D007536:Isomerism; D013058:Mass Spectrometry; D008745:Methylation; D008958:Models, Molecular; D010455:Peptides / Q000737:chemistry* / Q000378:metabolism; D017433:Protein Structure, Secondary; D011522:Protons; D011789:Quantum Theory; D013816:Thermodynamics
D010455:Peptides; D011522:Protons; D000805:Angiotensin III; D003035:Cobalt; D003300:Copper