Dissociation of peptide ions by fast atom bombardment in a quadrupole ion trap

Dissociation of peptide ions by fast atom bombardment in a quadrupole ion trap
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DOI:
10.1002/rcm.2038
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发表时间:
2005-01-01
影响因子:
2
通讯作者:
Zubarev, RA
Zubarev, RA
中科院分区:
化学3区
文献类型:
--
作者:
Misharin, AS;Silivra, OA;Zubarev, RA

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描述了一种用于离子阱(包括射频装置)中储存的多肽的阳离子和阴离子破碎的新技术。该技术涉及由快速原子轰击(FAB)枪产生的粒子束照射肽离子。这种辐照导致阳离子的N-C(α)主键(c-和z-片段)和S-S键断裂,阴离子的c (α)- c主键(a-和x-片段)断裂。观察到的碎片模式被假设是由于肽离子与由FAB枪产生的亚稳态电子激发的物质相互作用。亚稳原子a *与肽n阳离子M(n+)的相互作用导致电子通过形成离子对碰撞配合物a(+....)从亚稳原子转移到多阳离子。M((n-1)+.)和随后的肽阳离子断裂。因此,对于多阳离子,这种亚稳诱导的离子离解(MIDI)类似于电子捕获离解(ECD)现象。A*与阴离子的相互作用导致亚稳态物质的去激发和一个电子从阴离子上脱离。这反过来又导致类似于电子分离解离(EDD)的骨干断裂。MIDI技术稳健而高效,适用于2+或2-低电荷态的肽。版权所有(c) 2005 John Wiley & Sons, Ltd。
A new technique for fragmentation of cations and anions of peptides stored in ion traps including radiofrequency devices is described. The technique involves irradiation of peptide ions by a beam of particles generated by a fast atom bombardment (FAB) gun. This irradiation leads to fragmentation of N-C(alpha) backbone bonds (c- and z-fragments) and S-S bonds for cations and C(alpha)-C backbone bonds (a- and x-fragments) for anions of peptides. The fragmentation patterns observed are hypothesized to be due to the interaction of peptide ions with metastable, electronically excited species generated by the FAB gun. Interaction of a metastable atom A* with a peptide n-cation M(n+) leads to the electron transfer from the metastable atom to the polycation through the formation of an ion-pair collision complex A(+....) M((n-1)+.) and subsequent fragmentation of the peptide cation. Thus, for polycations, this metastable-induced dissociation of ions (MIDI) is similar to the phenomenon of electron capture dissociation (ECD). Interaction of A* with an anion leads to the deexcitation of the metastable species and detachment of an electron from the anion. This in turn leads to backbone fragmentation similar to that in electron detachment dissociation (EDD). The MIDI technique is robust and efficient, and it is applicable to peptides in as low charge states as 2+ or 2-. Copyright (c) 2005 John Wiley & Sons, Ltd.