Secondary fragmentation of linear peptides in electron capture dissociation

被引:72
作者
Cooper, HJ
Hudgins, RR
Håkansson, K
Marshall, AG
机构
[1] Florida State Univ, Ion Cyclotron Resonance Program, Natl High Magnet Field Lab, Tallahassee, FL 32310 USA
[2] Florida State Univ, Dept Chem & Biochem, Tallahassee, FL 32310 USA
关键词
FT-ICR; FT-MS; electron capture dissociation; ECD; secondary fragmentation; MS/MS; tandem MS;
D O I
10.1016/S1387-3806(03)00202-1
中图分类号
O64 [物理化学(理论化学)、化学物理学]; O56 [分子物理学、原子物理学];
学科分类号
070203 ; 070304 ; 081704 ; 1406 ;
摘要
inspection of the electron capture dissociation (ECD) spectra of doubly-protonated peptides, Leu(4)-Sar-Leu(3)-Lys-OH, Leu(4)-Ala-Leu(3)-Lys-OH, Gly(4)-Sar-Gly(3)-Lys-NH2 and Gly(3)-Pro-Sar-Gly(3)-Lys-NH2, reveals extensive secondary fragmentation. In addition to w ions, entire, and in some cases multiple, cleavages of amino acid side chains from backbone fragments are observed. Extensive water loss from backbone fragments is observed for the glycine-rich peptides. For Leu(4)-Ala-Leu(3)-Lys, the preferred fragmentation channel is cleavage of the amide bond to produce b(7) and b(8) ions. ECD of Gly(3)-Pro-Sar-Gly(3)-Lys-NH2 results in amine bond (c/z) cleavage in the proline residue accompanied by C-C (or secondary N-C) cleavage in the proline side chain. That fragmentation channel has not been observed previously. The peptides were also subjected to "hot" electron capture dissociation (RECD) and the resulting spectra differed markedly from those obtained under standard ECD conditions. In contrast to HECD, secondary fragmentation observed under standard ECD conditions cannot be attributed to excess energy arising from the kinetic energy of the electrons prior to capture. The results suggest that the fragmentation channels available following electron capture depend somewhat on the individual peptide structure and have mechanistic implications. (C) 2003 Elsevier Science B.V. All rights reserved.
引用
收藏
页码:723 / 728
页数:6
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