Factors that impact the vacuum ultraviolet photofragmentation of peptide ions

Thompson, Matthew S.; Cui, Weidong; Reilly, James P.

doi:10.1016/j.jasms.2007.04.015

Cited by 58 publications

(107 citation statements)

References 29 publications

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“…Melittin, kassinin, Lys [0]bradykinin, bradykinin, dynorphin-␤, GSK-␤ ␤ inhibitor, myosin kinase inhibitor, and mouse ANP [1][2][3][4][5][6][7][8][9][10][11] were purchased from American Peptide Company (Sunnyvale, CA). Polyalanine peptides were synthesized in-house using standard Fmoc coupling methodology.…”

Section: Methodsmentioning

confidence: 99%

“…It is demonstrated that a naphthyl based 18-crown-6 adduct is ideally suited for attaching to a variety peptides and fragmenting them following absorption of 266 nm light. [7][8][9][10][11]. Though none of these techniques is perfect, each has characteristic strengths and weaknesses.…”

mentioning

confidence: 99%

“…here are a variety of mainstream fragmentation methodologies available for interrogating peptides, including collision-induced dissociation (CID) [1], infrared multiphoton photodissociation (IRMPD) [2], electron capture dissociation (ECD) [3], and electron-transfer dissociation (ETD) [4]. In addition, there are other methods that can be used, such as surface induced dissociation (SID) [5], black-body infrared radiative dissociation (BIRD) [6], along with various photodissociation experiments employing high-energy lasers [7][8][9][10][11]. Though none of these techniques is perfect, each has characteristic strengths and weaknesses.…”

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confidence: 99%

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Rapid peptide fragmentation without electrons, collisions, infrared radiation, or native chromophores

Yeh

Sun

Meneses

et al. 2009

J. Am. Soc. Mass Spectrom.

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Ultraviolet photodissociation of peptides followed by mass analysis has several desirable advantages relative to other methods, yet it has not found widespread use due to several limitations. One shortcoming is the inefficiency with which peptides absorb in the ultraviolet. This issue has a simple solution and can be circumvented by the attachment of noncovalent adducts that contain appropriate chromophores. Subsequent photoactivation of the chromophore leads to vibrational excitation of the complex and eventually to fragmentation of the peptide. Herein, the energetics that control the efficiency of this process are examined as a function of the characteristics of both the peptide and the noncovalently attached chromophore. Fragmentation efficiency decreases with increasing peptide size and is also constrained by the binding energy of the noncovalent adduct. The optimum chromophore should have excellent absorption at the excitation wavelength and a low luminescence quantum yield. It is demonstrated that a naphthyl based 18-crown-6 adduct is ideally suited for attaching to a variety peptides and fragmenting them following absorption of 266 nm light. [7][8][9][10][11]. Though none of these techniques is perfect, each has characteristic strengths and weaknesses. For example CID is easily employed in the source region of any instrument with atmospheric pressure ionization. CID is also easily accommodated elsewhere in an instrument as long as high vacuum is not required. In contrast, IRMPD is well suited for collisionless environments. In this regard, CID and IRMPD provide complementary capabilities. Furthermore, since both methods fragment ions by the stepwise addition of small amounts of energy, the results obtained are frequently quite similar.However, CID and IRMPD are both limited by the fact that energy deposition occurs over a relatively long time scale, typically milliseconds to seconds. In contrast, ultraviolet photodissociation (UVPD) occurs on a much shorter time scale and can yield fragment ions characteristic of CID or IRMPD. However, the major limitation of UVPD is that the precursor ion must contain a suitable chromophore. For peptides, UVPD requires either short wavelength lasers (less than 200 nm) or peptides rich in tyrosine, tryptophan, and phenylalanine that can absorb at longer wavelengths. Therefore, UVPD is either limited to a small subset of all peptides or constrained by undesirable technical challenges which are encountered when working in the vacuum ultraviolet. Thus, widespread implementation of UVPD for peptide fragmentation has been to date somewhat limited.However, Brodbelt and coworkers have recently described a method to circumvent the requirement for aromatic residues or short wavelength lasers [12]. In this work, a noncovalently attached chromophore was used to absorb energy from a photon and transfer it to a peptide, causing the peptide to fragment. 18-crown-6 ether (18C6), which preferentially associates with lysine residues via the formation of three hydrogen bonds, was used for...

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Section: Methodsmentioning

confidence: 99%

mentioning

confidence: 99%

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confidence: 99%

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Rapid peptide fragmentation without electrons, collisions, infrared radiation, or native chromophores

Yeh

Sun

Meneses

et al. 2009

J. Am. Soc. Mass Spectrom.

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“…To combat these issues, significant interest has been placed in the development of new ion activation methods, such as electronic excitation dissociation (EED) [16], electron ionization dissociation (EID) [17], ultraviolet photodissociation (UVPD) [18,19], femtosecond laser-induced ionization/ dissociation (fs-LID) [20], action spectroscopy (synchrotron radiation) [21], and metastable atom-activated dissociation (MAD) [22,23]. These fragmentation methods all possess a common feature-the capability of dissociating low charge state (1+ & 2+) precursor ions, thus providing complementary structural information to ETD/ECD.…”

Section: Introductionmentioning

confidence: 99%

“…Contrary to the common ion/ion dissociation methods, CTD utilizes the interaction between homo-polarity ions such as peptide cations and helium cations, which, in the case of 1+ substance P, results in a dominant series of a ions. It has been widely reported that the fragmentation pattern of MS/MS techniques shows certain dependence on the charge state of precursor ions and the type of mass analyzer [14,19,25]. To investigate this dependence, CTD fragmentation of substance P and bradykinin at different charge states (1+, 2+, and 3+) was carried out in a 3D ion trap mass spectrometer.…”

Section: Introductionmentioning

confidence: 99%

Charge Transfer Dissociation (CTD) Mass Spectrometry of Peptide Cations: Study of Charge State Effects and Side-Chain Losses

Jackson

2017

J. Am. Soc. Mass Spectrom.

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Abstract. 1+, 2+, and 3+ precursors of substance P and bradykinin were subjected to helium cation irradiation in a 3D ion trap mass spectrometer. Charge exchange with the helium cations produces a variety of fragment ions, the number and type of which are dependent on the charge state of the precursor ions. For 1+ peptide precursors, fragmentation is generally restricted to C−CO backbone bonds (a and x ions), whereas for 2+ and 3+ peptide precursors, all three backbone bonds (C−CO, C−N, and N−Cα) are cleaved. The type of backbone bond cleavage is indicative of possible dissociation channels involved in CTD process, including high-energy, kinetic-based, and ETD-like pathways. In addition to backbone cleavages, amino acid side-chain cleavages are observed in CTD, which are consistent with other high-energy and radical-mediated techniques. The unique dissociation pattern and supplementary information available from side-chain cleavages make CTD a potentially useful activation method for the structural study of gas-phase biomolecules.

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Ion Activation Methods for Tandem Mass Spectrometry

Håkansson

Klassen

2010

Electrospray and MALDI Mass Spectrometry

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Factors that impact the vacuum ultraviolet photofragmentation of peptide ions

Cited by 58 publications

References 29 publications

Rapid peptide fragmentation without electrons, collisions, infrared radiation, or native chromophores

Rapid peptide fragmentation without electrons, collisions, infrared radiation, or native chromophores

Charge Transfer Dissociation (CTD) Mass Spectrometry of Peptide Cations: Study of Charge State Effects and Side-Chain Losses

Ion Activation Methods for Tandem Mass Spectrometry

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