Optimization of Guanidination Procedures for MALDI Mass Mapping

Beardsley, Richard L.; Reilly, James P.

doi:10.1021/ac015613o

Cited by 142 publications

(195 citation statements)

References 30 publications

(86 reference statements)

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“…Tryptic peptides were obtained by enzymatic digestion of proteins followed by HPLC purification. Guanidination of one lysine-containing peptide was performed according to the published procedure [39].…”

Section: Methodsmentioning

confidence: 99%

“…High-energy CID (Figure 6d) produces y-type ions, and some a-and b-type fragments are also present, but no x ions are observed. When this peptide is modified via a 1 h guanidination reaction [39], converting the lysine into homoarginine, the photodissociation spectrum (Figure 6e) resembles that of an arginine-containing peptide, with primarily x, v, and w ions accompanied by a few y ions.…”

Section: Lysine-terminated Peptidesmentioning

confidence: 99%

“…This leads to the observed scrambling of the charge site in the photodissociation spectrum and the occurrence of charge-induced secondary processes. Methods to increase the gas-phase basicity of lysine by conversion to homoarginine are available [39,60]. Similar to arginine-terminated peptides, these modified peptides yield a nearly full series of x ions together with multiple v-and w-type ions (Figure 6e).…”

Section: Role Of Argininementioning

confidence: 99%

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Pathways of Peptide Ion Fragmentation Induced by Vacuum Ultraviolet Light

Cui

Thompson

Reilly

2005

J. Am. Soc. Mass Spectrom.

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116

181

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One Hundred Fifty-Seven nm photodissociation of singly protonated peptides generates unusual distributions of fragment ions. When the charge is localized at the C-terminus of the peptide, spectra are dominated by x-, v-, and w-type fragments. When it is sequestered at the N-terminus, a-and d-type ions are overwhelmingly abundant. Evidence is presented suggesting that the fragmentation occurs via photolytic radical cleavage of the peptide backbone at the bond between the ␣-and carbonyl-carbons followed by radical elimination to form the observed daughter ions. Low-energy fragmentation appears to be well described by the mobile proton model according to which vibrational excitation of the analyte leads to charge mobility [12]. Transfer of the charge proton to either the backbone carbonyl oxygen or amide nitrogen enables charge-induced cleavage of the peptide backbone. This process yields primarily b-and y-type fragment ions according to the standard nomenclature shown below [13,14].Higher energy activation methods involving collisions with gas molecules or surfaces can enable chargeremote fragmentation [15][16][17]. However, even in these cases, apparently, protonated peptides still generate some fragments through charge-directed processes [17]. Immobilization of the charge, either by using metal adducts [18] or charged chemical modifications [19 -22], has been used to inhibit charge-directed fragmentation. In these cases, primarily a-, d-, and w-type fragments are observed. Several mechanisms have been proposed for charge-remote peptide fragmentation, some involving homolytic radical cleavage [14,23].Electron capture dissociation (ECD) [24] and the recently reported electron-transfer dissociation (ETD)[25] appear to be nonthermal processes. These phenomena generate c-and z-type fragment ions upon the addition of an electron to a multiply charged protein or peptide ion. Two mechanisms have been proposed, one involving reactions of a free hydrogen atom generated when an electron is captured by a charged site on the analyte ion [26], and the other involving localization of the ϳ6 eV of energy that is generated upon charge neutralization. This energy then induces fragmentation through an excited electronic state [27]. Implicit in this second mechanism is the suggestion that techniques which excite appropriate electronic states can lead to unique, nonergodic fragmentation even for molecules as large as peptides and proteins [24,27]. This can occur if ions reach a dissociative electronic state and fragment before the energy is redistributed throughout the molecule. Electronic to vibrational relaxation, resulting in nonspecific excitation is an important competing process that often inhibits nonergodic processes, and rates of relaxation are predicted to increase with the size of the molecule [28].Lasers are powerful tools that can also be used to excite molecules to specific energy levels with either multiphoton or single photon processes. Light is not affected by the electric or magnetic fields of mass spectrometers, s...

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Section: Methodsmentioning

confidence: 99%

Section: Lysine-terminated Peptidesmentioning

confidence: 99%

Section: Role Of Argininementioning

confidence: 99%

See 1 more Smart Citation

Pathways of Peptide Ion Fragmentation Induced by Vacuum Ultraviolet Light

Cui

Thompson

Reilly

2005

J. Am. Soc. Mass Spectrom.

Self Cite

116

181

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“…Such approaches include ICAT and its modifications (4 -7), acrylamide labeling (8), 18 O-labeling during proteolysis (9,10), and guanidination of lysine residues (11)(12)(13). In all of these approaches, the degree of labeling is controlled by the isotope enrichment of the labeling reagent and the completeness of the modification chemistry and is applied to proteins or protein mixtures obtained after cell disruption.…”

mentioning

confidence: 99%

Metabolic Labeling of Proteins for Proteomics

Beynon

Pratt

2005

Molecular & Cellular Proteomics

189

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“…Several charge tags have been investigated on the basis of their chemical availability or synthetic convenience, e.g., 2,4,6-trimethylpyridinium [4], 2,2'-bipyridyl [5], tris(2,4,6-trimethoxyphenyl)phosphonium (TMPP) [6][7][8], and trimethylammoniumalkyl [9,10]. Enhanced charging can also be achieved by introducing into the peptide the basic guanidine group by various guanidination strategies [11][12][13][14][15][16][17]. There are several criteria that the charge tags should meet.…”

mentioning

confidence: 99%

Tunable Charge Tags for Electron-Based Methods of Peptide Sequencing: Design and Applications

Zimnicka

Moss

Chung

et al. 2011

J. Am. Soc. Mass Spectrom.

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Charge tags using basic auxiliary functional groups 6-aminoquinolinylcarboxamido, 4-aminopyrimidyl-1-methylcarboxamido, 2-aminobenzoimidazolyl-1-methylcarboxamido, and the fixedcharge 4-(dimethylamino)pyridyl-1-carboxamido moiety are evaluated as to their properties in electron transfer dissociation mass spectra of arginine C-terminated peptides. The neutral tags have proton affinities that are competitive with those of amino acid residues in peptides. Charge reduction by electron transfer from fluoranthene anion-radicals results in peptide backbone dissociations that improve sequence coverage by providing extensive series of N-terminal ctype fragments without impeding the formation of C-terminal z fragments. Comparison of ETD mass spectra of free and tagged peptides allows one to resolve ambiguities in fragment ion assignment through mass shifts of c ions. Simple chemical procedures are reported for Nterminal tagging of Arg-containing tryptic peptides.

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Optimization of Guanidination Procedures for MALDI Mass Mapping

Cited by 142 publications

References 30 publications

Pathways of Peptide Ion Fragmentation Induced by Vacuum Ultraviolet Light

Pathways of Peptide Ion Fragmentation Induced by Vacuum Ultraviolet Light

Metabolic Labeling of Proteins for Proteomics

Tunable Charge Tags for Electron-Based Methods of Peptide Sequencing: Design and Applications

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