Changes in Dissociation Efficiency and Kinetics of Peptide Ions Induced by Basic Residues and Their Mechanistic Implication |
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Authors: | So Hee Yoon Jeong Hee Moon Myung Soo Kim |
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Institution: | Department of Chemistry, Seoul National University, Seoul, Korea. |
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Abstract: | With matrix-assisted laser desorption ionization (MALDI) time-of-flight (TOF) mass spectrometry, total abundance of product
ions formed by dissociation inside (in-source decay, ISD) and outside (post-source decay, PSD) the source was measured for
peptide ions Y
5
X + H]+, XY
5 + H]+, Y
2
XY
3 + H]+, and XY
4
X + H]+ (X = tyrosine (Y), histidine (H), lysine (K), and arginine (R) with H for the ionizing proton). α-Cyano-4-hydroxycinammic acid was used as matrix. Product abundance became smaller in
the presence of basic residues (H, K, and R), in the order Y > H ≈ K > R. In particular, product abundances in ISD of peptide ions with R were smaller than those with H or K by an order of magnitude, which, in turn, were smaller than that for Y
6 + H]+ by an order of magnitude. Product abundance was affected by the most basic residue when more than one basic residue was present.
A kinetic explanation for the data was attempted under the assumption of quasi-thermal equilibrium for peptide ions in MALDI
plume which undergoes expansion cooling. Dramatic disparity in product abundance was found to arise from small difference
in critical energy and entropy. Results indicate similar transition structures regardless of basic residues present, where
the ionizing proton keeps interacting with a basic site. Further implication of the results on the dissociation mechanism
along b-y channels is discussed. |
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Keywords: | |
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