Protein sequence information by matrix‐assisted laser desorption/ionization in‐source decay mass spectrometry

Hardouin, Julie

doi:10.1002/mas.20142

Cited by 139 publications

(147 citation statements)

References 110 publications

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“…The in-source formation of CID-like fragments by the thermal pathway has not been widely studied [33]. Because this thermal process is caused by vibrational activation of closed valence shell ions, the fragmentation mechanism can be explained by the "mobile proton" model [34].…”

Section: Influence Of the Matrixmentioning

confidence: 99%

MALDI In-Source Decay, from Sequencing to Imaging

Debois

Smargiasso

Demeure

et al. 2012

Topics in Current Chemistry

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Matrix-assisted laser desorption/ionization (MALDI) is now a mature method allowing the identification and, more challenging, the quantification of biopolymers (proteins, nucleic acids, glycans, etc). MALDI spectra show mostly intact singly charged ions. To obtain fragments, the activation of singly charged precursors is necessary, but not efficient above 3.5 kDa, thus making MALDI MS/MS difficult for large species. In-source decay (ISD) is a prompt fragmentation reaction that can be induced thermally or by radicals. As fragments are formed in the source, precursor ions cannot be selected; however, the technique is not limited by the mass of the analyzed compounds and pseudo MS3 can be performed on intense fragments. The discovery of new matrices that enhance the ISD yield, combined with the high sensitivity of MALDI mass spectrometers, and software development, opens new perspectives. We first review the mechanisms involved in the ISD processes, then discuss ISD applications like top-down sequencing and post-translational modifications (PTMs) studies, and finally review MALDI-ISD tissue imaging applications.

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Section: Influence Of the Matrixmentioning

confidence: 99%

MALDI In-Source Decay, from Sequencing to Imaging

Debois

Smargiasso

Demeure

et al. 2012

Topics in Current Chemistry

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“…The resulting spectra are very simple and the analysis of the sequences and PTM sites is straightforward. Therefore, the use of ESI-ECD/ETD and MALDI-ISD have been utilized as tools in the top-down approach for proteomics [11,15].…”

mentioning

confidence: 99%

In-source decay and fragmentation characteristics of peptides using 5-aminosalicylic acid as a matrix in matrix-assisted laser desorption/ionization mass spectrometry

Sakakura

Takayama

2010

J. Am. Soc. Mass Spectrom.

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The use of 5-aminosalicylic acid (5-ASA) as a new matrix for in-source decay (ISD) of peptides including mono-and di-phosphorylated peptides in matrix-assisted laser desorption/ionization (MALDI) mass spectrometry (MS) is described. The use of 5-ASA in MALDI-ISD has been evaluated from several standpoints: hydrogen-donating ability, the outstanding sharpness of molecular and fragment ion peaks, and the presence of interference peaks such as metastable peaks and multiply charged ions. The hydrogen-donating ability of several matrices such as ␣-cyano-4-hydroxycinnamic acid (CHCA), 2,5-dihydroxybenzoic acid (2,5-DHB), 1,5-diaminonaphthalene (1,5-DAN), sinapinic acid (SA), and 5-ASA was evaluated by using the peak abundance of a reduction product [M ϩ 2H ϩ H] ϩ to that of non-reduced protonated molecule [M ϩ H] ϩ of the cyclic peptide vasopressin which contains a disulfide bond (S-S). The order of hydrogendonating ability was 1,5-DAN Ͼ 5-ASA Ͼ 2,5-DHB Ͼ SA ϭ CHCA. The chemicals 1,5-DAN and 5-ASA in particular can be classified as reductive matrices. 5-ASA gave peaks with higher sharpness for protonated molecules and fragment ions than other matrices and did not give any interference peaks such as multiply-protonated ions and metastable ions in the ISD mass spectra of the peptides used. Particularly, 1,5-DAN and 5-ASA gave very little metastable peaks. This indicates that 1,5-DAN and 5-ASA are more "cool" than other matrices. The 1,5-DAN and 5-ASA can therefore be termed "reductive cool" matrix. T he role of mass spectrometry (MS) in protein sciences such as proteomics has become increasingly important due to its outstanding sensitivity and rapidity. It is of importance to recognize that the analysis of proteins using MS generally pertains to the analysis of peptides obtained upon enzymatic digestion of proteins. MS coupled to soft ionization methods such as matrix-assisted laser desorption/ionization (MALDI) [1][2][3] and electrospray ionization (ESI) [4,5] have been used to obtain qualitative information for peptide-mass fingerprinting (PMF), amino acid sequencing and analysis of post-translational modifications (PTMs), and quantitative information about protein(s) expressed from a genome [6,7]. The most valuable information for protein identification including PTMs is the amino acid sequences that are available from tandem mass spectrometry and other MS degradation methods.Of the mass spectrometric dissociation methods used for identifying proteins, electron capture dissociation (ECD) [8] and electron-transfer dissociation (ETD) [9] coupled to ESI and in-source decay (ISD) coupled to MALDI [10] have been noted from the standpoint of specific cleavage at the N-C␣ bond on the peptide backbone because conventional methods such as collision-induced dissociation (CID) leads to nonspecific cleavage of the peptide backbone and the loss of PTM functional groups [11]. The nonspecific cleavage gives backbone cleaved fragments such as a-, b-, x-, and y-series ions (Scheme 1 upper [12] and the loss of NH 3 and/or H 2 O from t...

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“…39–41 Takayama et al 42 described this mechanism as a hydrogen radical transfer from the matrix to the peptide bond carbonyl group, followed by radical ion rearrangements that predominantly yield c- and z + 2 ions. Based on this concept, MALDI-ISD has been used for protein and peptide sequencing, disulfide bond identification, localization of post-translation modifications (PTMs), and de novo sequencing of a 13.6 kDa protein.…”

Section: Introductionmentioning

confidence: 99%

Rapid, automated characterization of disulfide bond scrambling and IgG2 isoform determination

Resemann

Liu-Shin

Tremintin

et al. 2018

mAbs

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Human antibodies of the IgG2 subclass exhibit complex inter-chain disulfide bonding patterns that result in three structures, namely A, A/B, and B. In therapeutic applications, the distribution of disulfide isoforms is a critical product quality attribute because each configuration affects higher order structure, stability, isoelectric point, and antigen binding. The current standard for quantification of IgG2 disulfide isoform distribution is based on chromatographic or electrophoretic techniques that require additional characterization using mass spectrometry (MS)-based methods to confirm disulfide linkages. Detailed characterization of the IgG2 disulfide linkages often involve MS/MS approaches that include electrospray ionization or electron-transfer dissociation, and method optimization is often cumbersome due to the large size and heterogeneity of the disulfide-bonded peptides. As reported here, we developed a rapid LC-MALDI-TOF/TOF workflow that can both identify the IgG2 disulfide linkages and provide a semi-quantitative assessment of the distribution of the disulfide isoforms. We established signature disulfide-bonded IgG2 hinge peptides that correspond to the A, A/B, and B disulfide isoforms and can be applied to the fast classification of IgG2 isoforms in heterogeneous mixtures.

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Protein sequence information by matrix‐assisted laser desorption/ionization in‐source decay mass spectrometry

Cited by 139 publications

References 110 publications

MALDI In-Source Decay, from Sequencing to Imaging

MALDI In-Source Decay, from Sequencing to Imaging

In-source decay and fragmentation characteristics of peptides using 5-aminosalicylic acid as a matrix in matrix-assisted laser desorption/ionization mass spectrometry

Rapid, automated characterization of disulfide bond scrambling and IgG2 isoform determination

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