Effect of the Basic Residue on the Energetics, Dynamics, and Mechanisms of Gas-Phase Fragmentation of Protonated Peptides
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- 作者：Julia Laskin ; Zhibo Yang ; Tao Song ; Corey Lam ; Ivan K. Chu
- 刊名：Journal of the American Chemical Society
- 出版年：2010
- 出版时间：November 17, 2010
- 年：2010
- 卷：132
- 期：45
- 页码：16006-16016
- 全文大小：442K
- 年卷期：v.132,no.45(November 17, 2010)
- ISSN：1520-5126
文摘
The effect of the basic residue on the energetics, dynamics, and mechanisms of backbone fragmentation of protonated peptides was investigated. Time-resolved and collision energy-resolved surface-induced dissociation (SID) of singly protonated peptides with the N-terminal arginine residue and their analogues, in which arginine is replaced with less basic lysine and histidine residues, was examined using a specially configured Fourier transform ion cyclotron resonance mass spectrometer (FTICR-MS). SID experiments demonstrated different kinetics of formation of several primary product ions of peptides with and without arginine residue. The energetics and dynamics of these pathways were determined from Rice−Ramsperger−Kassel−Marcus (RRKM) modeling of the experimental data. Comparison between the kinetics and energetics of fragmentation of arginine-containing peptides and the corresponding methyl ester derivatives provides important information on the effect of dissociation pathways involving salt bridge (SB) intermediates on the observed fragmentation behavior. Because pathways involving SB intermediates are characterized by low threshold energies, they efficiently compete with classical oxazolone and imine/enol pathways of arginine-containing peptides on a long time scale of the FTICR instrument. In contrast, fragmentation of histidine- and lysine-containing peptides is largely determined by canonical pathways. Because SB pathways are characterized by negative activation entropies, fragmentation of arginine-containing peptides is kinetically hindered and observed at higher collision energies as compared to their lysine- and histidine-containing analogues.