High-energy electron transfer dissociation (HE-ETD) using alkali metal targets for sequence analysis of post-translational peptides

Hayakawa, Shigeo; Matsumoto, Shinya; Hashimoto, Mami; Iwamoto, Kaoru; Nagao, Hirofumi; Toyoda, Michisato; Shigeri, Yasushi; Tajiri, Michiko; Wada, Yoshinao

doi:10.1016/j.jasms.2010.05.010

Cited by 8 publications

(6 citation statements)

References 51 publications

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“…However, it has also been reported that the presence of phosphorylated serine residues hampered backbone dissociations of several synthetic peptides [16]. Electron transfer from alkali metal atoms has been reported recently to induce dissociations yielding sequence fragments from phosphopeptides [17,18].…”

Section: Introductionmentioning

confidence: 99%

Dipole-Guided Electron Capture Causes Abnormal Dissociations of Phosphorylated Pentapeptides

Moss

Chung

Wyer

et al. 2011

J. Am. Soc. Mass Spectrom.

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Electron transfer and capture mass spectra of a series of doubly charged ions that were phosphorylated pentapeptides of a tryptic type (pS,A,A,A,R) showed conspicuous differences in dissociations of charge-reduced ions. Electron transfer from both gaseous cesium atoms at 100 keV kinetic energies and fluoranthene anion radicals in an ion trap resulted in the loss of a hydrogen atom, ammonia, and backbone cleavages forming complete series of sequence z ions. Elimination of phosphoric acid was negligible. In contrast, capture of lowenergy electrons by doubly charged ions in a Penning ion trap induced loss of a hydrogen atom followed by elimination of phosphoric acid as the dominant dissociation channel. Backbone dissociations of charge-reduced ions also occurred but were accompanied by extensive fragmentation of the primary products. z-Ions that were terminated with a deaminated phosphoserine radical competitively eliminated phosphoric acid and H 2 PO 4 radicals. A mechanism is proposed for this novel dissociation on the basis of a computational analysis of reaction pathways and transition states. Electronic structure theory calculations in combination with extensive molecular dynamics mapping of the potential energy surface provided structures for the precursor phosphopeptide dications. Electron attachment produces a multitude of low lying electronic states in charge-reduced ions that determine their reactivity in backbone dissociations and H-atom loss. The predominant loss of H atoms in ECD is explained by a distortion of the Rydberg orbital space by the strong dipolar field of the peptide dication framework. The dipolar field steers the incoming electron to preferentially attach to the positively charged arginine side chain to form guanidinium radicals and trigger their dissociations.

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Section: Introductionmentioning

confidence: 99%

Dipole-Guided Electron Capture Causes Abnormal Dissociations of Phosphorylated Pentapeptides

Moss

Chung

Wyer

et al. 2011

J. Am. Soc. Mass Spectrom.

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“…68) Experimental results for high-energy collision induced dissociation (HE-CID) using the Xe and Cs targets were obtained for doubly-phosphorylated peptides TGFLT(p) EY(p) VATR (1). While the most abundant product ions in the case of the Xe target were immonium ions and doubly-charged fragment ions, charge-reduced fragment ions were produced in the case of the Cs target, whose relative abundances were about ten times larger than those of the immonium ions and the doubly-charged fragment ions.…”

Section: He-etd Of Peptides With Post-translational Modificationsmentioning

confidence: 99%

“…In order to examine the di erences in the ETD spectra depending on the MS/MS instrument, ETD spectra of a doubly protonated phosphopeptide were obtained by TOF/TOF, the sector type and the ion trap, where HE-ETD and LE-ETD spectra were identical, as reported in previous studies, 67,68) respectively. Figure 5 shows enlarged CID spectra of the doubly protonated phosphopeptide (YGGMHRQET(p) VDC) ions, (a): measured using the TOF/TOF instrument with a Cs target and (b): by using a sector type MS/MS instrument with a Cs target.…”

Section: He-etd Of Peptides With Post-translational Modificationsmentioning

confidence: 99%

Study of Ion Dynamics by Electron Transfer Dissociation: Alkali Metals as Targets

Hayakawa

2017

Mass Spectrometry

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High energy collision processes for singly charged positive ions using an alkali metal target are con rmed, as a charge inversion mass spectrometry, to occur by electron transfers in successive collisions and the dissociation processes involve the formation of energy-selected neutral species from near-resonant neutralization with alkali metal targets. A doubly charged thermometer molecule was made to collide with alkali metal targets to give singly and doubly charged positive ions. e internal energy resulting from the electron transfer with the alkali metal target was very narrow and centered at a particular energy. is narrow internal energy distribution can be attributed to electron transfer by Landau-Zener potential crossing between the precursor ion and an alkali metal atom, and the coulombic repulsion between singly charged ions in the exit channel. A large cross section of more than 10 −14 cm 2 was estimated for high-energy electron transfer dissociation (HE-ETD). Doubly protonated phosphorylated peptides obtained by electrospray ionization were collided with Xe and Cs targets to give singly and doubly charged positive ions. Whereas doubly charged fragment ions resulting from CAD were dominant in the case of the Xe target, singly charged fragment ions resulting from ETD were dominant with the Cs target. HE-ETD using the Cs target provided all of the z-type ions by N-C α bond cleavage without the loss of the phosphate groups. e results demonstrate that HE-ETD with an alkali metal target allowed the position of phosphorylation and the amino acid sequence of peptides with post translational modi cations (PTM) to be determined.

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“…Electron‐induced dissociation techniques, such as electron capture dissociation (ECD) and electron transfer dissociation (ETD), usually preserve the site of phosphorylation due to more random and nonergodic fragmentation. Several studies on protonated peptides and protein ions have demonstrated the ability of ECD and ETD to provide abundant sequence information as well as the location of phosphorylated sites . However, ECD and ETD can be limited by the fact that these processes generally require ions with a charge of 2+ or greater since capture or transfer of an electron to the charged species occurs.…”

Section: Introductionmentioning

confidence: 99%

“…Several studies on protonated peptides and protein ions have demonstrated the ability of ECD and ETD to provide abundant sequence information as well as the location of phosphorylated sites. 6,[16][17][18][19][20][21][22][23][24] However, ECD and ETD can be limited by the fact that these processes generally require ions with a charge of 2+ or greater since capture or transfer of an electron to the charged species occurs. Addition of an electron to a singly charged ion (1+) would result in a neutral molecule that cannot be analyzed by MS.…”

Section: Introductionmentioning

confidence: 99%

Electron transfer dissociation mass spectrometry of acidic phosphorylated peptides cationized with trivalent praseodymium

Commodore

Cassady

2018

J Mass Spectrom

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The lanthanide ion praseodymium, Pr (III), was employed to study metallated ion formation and electron transfer dissociation (ETD) of twenty-seven biological and model highly acidic phosphopeptides. All phosphopeptides investigated form metallated ions by electrospray ionization (ESI) that can be studied by ETD to yield abundant sequence information. The ions formed are [M + Pr - H] , [M + Pr] , and [M + Pr + H] . All biological phosphopeptide with a chain length of seven or more residues generate [M + Pr] . For biological phosphopeptides, [M + Pr] undergoes more backbone cleavage by ETD than [M + Pr - H] and, in some cases, full sequence coverage occurs. Acidic model phosphorylated hexa- and octa-peptides, composed of alanine residues and one phosphorylated residue, form exclusively [M + Pr - H] by ESI. Limited sequence information is obtained by ETD of [M + Pr - H] with only metallated product ions being generated. For two biological phosphopeptides, [M + Pr + H] is observed and may be due to the presence of at least one residue with a highly basic side chain that facilitates the addition of an extra proton. For the model phosphopeptides, more sequence coverage occurs when the phosphorylated residue is in the middle of the sequence than at either the N- or C-terminus. ETD of the metallated precursor ions formed by ESI generates exclusively metallated and non-metallated c- and z-ions for the biological phosphopeptides, while metallated c-, z-ions and a few y-ions form for the model phosphopeptides. Most of the product ions contain the phosphorylated residue indicating that the metal ion binds predominantly at the deprotonated phosphate group. The results of this study indicate that ETD is a promising tool for sequencing highly acidic phosphorylated peptides by metal adduction with Pr (III) and, by extension, all non-radioactive lanthanide metal ions.

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High-energy electron transfer dissociation (HE-ETD) using alkali metal targets for sequence analysis of post-translational peptides

Cited by 8 publications

References 51 publications

Dipole-Guided Electron Capture Causes Abnormal Dissociations of Phosphorylated Pentapeptides

Dipole-Guided Electron Capture Causes Abnormal Dissociations of Phosphorylated Pentapeptides

Study of Ion Dynamics by Electron Transfer Dissociation: Alkali Metals as Targets

Electron transfer dissociation mass spectrometry of acidic phosphorylated peptides cationized with trivalent praseodymium

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