Disulfide bond cleavage in TEMPO‐free radical initiated peptide sequencing mass spectrometry

Lee, Minhee; Lee, Younjin; Kang, Minhyuk; Park, Hyeyeon; Seong, Yeonmi; Sung, Bong June; Moon, Bongjin; Oh, Han Bin

doi:10.1002/jms.1955

Cited by 50 publications

(76 citation statements)

References 74 publications

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“…[23][24][25] In brief, the peptides of interest was dissolved in a 0.1 M NaHCO 3 buffer solution and then subjected to conjugation with o-TEMPO-Bz-NHS in DMSO by mixing. The o-TEMPO-Bz-conjugated peptides were purified prior to tandem mass spectrometry application, using the reversedphase solid phase extraction (SPE, Ultra-micro spin column C-18, Harvard Bioscience, Holliston, MA, USA) protocol.…”

Section: Methodsmentioning

confidence: 99%

Charge-Directed Peptide Backbone Dissociations of o-TEMPO-Bz-C(O)-Peptides

Jeon¹,

Lee²,

Kwon³

et al. 2013

Mass Spectrometry Letters

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In the present study, we report that the charge-directed (assisted) peptide dissociation products, such as b-and y-type peptide backbone fragments, were the major products in MS/MS and MS 3 applications of some o-TEMPO-Bz-C(O)-peptide ions, while radical-driven dissociation products, such as a/x and c/z-type fragments, were previously shown to be the major products in the free radical initiated peptide sequencing mass spectrometry (FRIPS MS). Those o-TEMPO-Bz-C(O)-peptides share a common feature in their sequences, that is, the peptides do not include an arginine residue that has the highest proton affinity among free amino acids. The appearance of b-and y-type fragments as major products in FRIPS MS can be understood in terms of the so-called "mobile-proton model". When the proton is highly mobilized by the absence of arginine, the chare-directed peptide dissociation pathways appear to be more competitive than the radical-driven dissociation pathways, in our FRIPS experiments.

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Section: Methodsmentioning

confidence: 99%

Charge-Directed Peptide Backbone Dissociations of o-TEMPO-Bz-C(O)-Peptides

Jeon¹,

Lee²,

Kwon³

et al. 2013

Mass Spectrometry Letters

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“…Collisional activation of such radical ions results in side-chain and backbone cleavage with extensive sequence coverage. Lee et al introduced 2-[(2,2,6,6-tetramethylpiperidin-1-oxyl)methyl]benzoic acid (TEMPO-Bz, Scheme 1) as a free radical precursor bound to peptides through the N-terminus or at the ε-amine of lysine residues, [27][28][29] and is the tagging group employed in the present study. Collisional activation of the precursor peptide ions initiates homolytic cleavage of the labile NO-C bond, promoted by the remarkable stability of the released nitroxyl radical.…”

Section: Introductionmentioning

confidence: 99%

Photodissociation of TEMPO-modified peptides: new approaches to radical-directed dissociation of biomolecules

Marshall

Hansen

Trevitt

et al. 2014

Phys. Chem. Chem. Phys.

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Photodissociation of TEMPO-modified peptides: new approaches to radical-directed dissociation of biomolecules AbstractRadical-directed dissociation of gas phase ions is emerging as a powerful and complementary alternative to traditional tandem mass spectrometric techniques for biomolecular structural analysis. Previous studies have identified that coupling of 2-[(2,2,6,6-tetramethylpiperidin-1-oxyl)methyl]benzoic acid (TEMPO-Bz) to the N-terminus of a peptide introduces a labile oxygen-carbon bond that can be selectively activated upon collisional activation to produce a radical ion. Here we demonstrate that structurally-defined peptide radical ions can also be generated upon UV laser photodissociation of the same TEMPO-Bz derivatives in a linear ion-trap mass spectrometer. When subjected to further mass spectrometric analyses, the radical ions formed by a single laser pulse undergo identical dissociations as those formed by collisional activation of the same precursor ion, and can thus be used to derive molecular structure. Mapping the initial radical formation process as a function of photon energy by photodissociation action spectroscopy reveals that photoproduct formation is selective but occurs only in modest yield across the wavelength range (300-220 nm), with the photoproduct yield maximised between 235 and 225 nm. Based on the analysis of a set of model compounds, structural modifications to the TEMPO-Bz derivative are suggested to optimise radical photoproduct yield. Future development of such probes offers the advantage of increased sensitivity and selectivity for radicaldirected dissociation. AbstractRadical-directed dissociation of gas phase ions is emerging as a powerful and complementary alternative to traditional tandem mass spectrometric techniques for biomolecular structural analysis. Previous studies have identified that coupling of 2-[(2,2,6,6-tetramethylpiperidin-1-oxyl)methyl]benzoic acid (TEMPO-Bz) to the N-terminus of a peptide introduces a labile oxygen-carbon bond that can be selectively activated upon collisional activation to produce a radical ion. Here we demonstrate that structurally-defined peptide radical ions can also be generated upon UV laser photodissociation of the same TEMPO-Bz derivatives in a linear ion-trap mass spectrometer. When subjected to further mass spectrometric analyses, the radical ions formed by a single laser pulse undergo identical dissociations as those formed by collisional activation of the same precursor ion, and can thus be used to derive molecular structure. Mapping the initial radical formation process as a function of photon energy by photodissociation action spectroscopy reveals that photoproduct formation is selective but occurs only in modest yield across the wavelength range (300 -220 nm), with the photoproduct yield maximised between 235 and 225 nm. Based on the analysis of a set of model compounds, structural modifications to the TEMPO-Bz derivative are suggested to optimise radical photoproduct yield. Future development of such probes offers t...

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“…43,44 Another innovative approach is the development of the so-called free radical initiated peptide sequencing mass spectrometry (FRIPS-MS). [45][46][47][48][49] In FRIPS, a radical precursor is incorporated as a † This paper is to commemorate Professor Myung Soo Kim's honourable retirement.…”

Section: -42mentioning

confidence: 99%

“…Furthermore, the TEMPO-based FRIPS approach was shown to lead to the rupture of the disulfide (S-S) or the adjacent C-S bond in an exclusive manner, prior to peptide backbone dissociations. 48 Very recently, it was found that in negative ion mode, the radical-driven peptide backbone dissociations can be achieved in a single step, in contrast to the two-step peptide dissociations in positive ion mode. 49 The relative collision energy requirements for the two thermal activation steps in the TEMPO-based FRIPS were found to be responsible for the different peptide sequencing behaviors in the positive-and negative-ion modes.…”

Section: -49mentioning

confidence: 99%

Density Functional Theory (DFT) Study of Gas-phase O.C Bond Dissociation Energy of Models for o-TEMPO-Bz-C(O)-Peptide: A Model Study for Free Radical Initiated Peptide Sequencing

Kwon¹,

Kwon²,

Lee³

et al. 2014

Bulletin of the Korean Chemical Society

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The bond dissociation energy (BDE) of the chemical bond between the carbon and oxygen atoms of a simple TEMPO-derivative is calculated by employing the density functional theory, the 2 nd order Møller-Plesset (MP2) perturbation theory, and complete basis set (CBS) methods. We find that BDE of the positive ion of the TEMPO-derivative is larger at least by 7 kcal/mol than that of the negative ion, which implies that the dissociation reaction rate of the positive ion should be slower than that of the negative ion. Such theoretical predictions are contrary to the results of our previous experiments (Anal. Chem. 2013, 85, 7044), in which the larger energy was required for negative o-TEMPO-Bz-C(O)-peptides to undergo the dissociation reactions than for the positive ones. By comparing our theoretical results to those of the experiments, we conclude that the dissociation reaction of o-TEMPO-Bz-C(O)-peptide should occur in a complicated fashion with a charge, either positive or negative, probably being located on the amino acid residues of the peptide.

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Disulfide bond cleavage in TEMPO‐free radical initiated peptide sequencing mass spectrometry

Cited by 50 publications

References 74 publications

Charge-Directed Peptide Backbone Dissociations of o-TEMPO-Bz-C(O)-Peptides

Charge-Directed Peptide Backbone Dissociations of o-TEMPO-Bz-C(O)-Peptides

Photodissociation of TEMPO-modified peptides: new approaches to radical-directed dissociation of biomolecules

Density Functional Theory (DFT) Study of Gas-phase O.C Bond Dissociation Energy of Models for o-TEMPO-Bz-C(O)-Peptide: A Model Study for Free Radical Initiated Peptide Sequencing

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