A Simple Solid Phase Mass Tagging Approach for Quantitative Proteomics

Yang, Sen; Xiang, Rong; Crawford, Janet; Colangelo, Christopher M.; Horváth, Csaba; Wilkins, James A.

doi:10.1021/pr034081k

Cited by 43 publications

(44 citation statements)

References 12 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…The cICAT (Hansen et al, 2003;Oda et al, 2003) Other cysteine-specific affinity tags for quantitative proteomics have been introduced based on solid-phase capture approaches, like the acid-labile isotope-coded extractants (ALICE) (Qiu et al, 2002). Isotopic solid-phase mass tagging was also developed for capture on polymethacrylate/PEG resin (Shi et al, 2004(Shi et al, , 2005. The solid-phase mass tags permitted: (i) the tagging of cysteine-containing peptides via its iodoacetyl group, (ii) the introduction of stable isotopes with a tri-alanine moiety that contained either 12 C or 13 C, (iii) the isolation of the tagged peptides via the attachment to a methacrylate resin, and (iv) the release due to an acid-labile linker group.…”

Section: Combined Quantitative Methodsmentioning

confidence: 99%

Cysteine tagging for MS‐based proteomics

Giron

Dayon

Sanchez

2010

Mass Spectrometry Reviews

View full text Add to dashboard Cite

Amino acid-tagging strategies are widespread in proteomics. Because of the central role of mass spectrometry (MS) as a detection technique in protein sciences, the term "mass tagging" was coined to describe the attachment of a label, which serves MS analysis and/or adds analytical value to the measurements. These so-called mass tags can be used for separation, enrichment, detection, and quantitation of peptides and proteins. In this context, cysteine is a frequent target for modifications because the thiol function can react specifically by nucleophilic substitution or addition. Furthermore, cysteines present natural modifications of biological importance and a low occurrence in the proteome that justify the development of strategies to specifically target them in peptides or proteins. In the present review, the mass-tagging methods directed to cysteine residues are comprehensively discussed, and the advantages and drawbacks of these strategies are addressed. Some concrete applications are given to underline the relevance of cysteine-tagging techniques for MS-based proteomics.

show abstract

Section: Combined Quantitative Methodsmentioning

confidence: 99%

Cysteine tagging for MS‐based proteomics

Giron

Dayon

Sanchez

2010

Mass Spectrometry Reviews

View full text Add to dashboard Cite

show abstract

“…Following the initial success of the ICAT approach, several variations on this chemical reagent class emerged to improve, e.g., recovery of labeled peptides or chromatographic properties [28][29][30][31]. Other thiol-specific reagents typically contain halogen-substituted carboxylic acids or amides [32][33][34][35] or employ the Michael-type addition reaction to carbonyl groups (e.g., maleiimide esters and vinylpyridine) [36,37]. As cysteine is a rare amino acid, ICAT and related methods significantly reduce the complexity of the peptide mixture which can be advantageous when highly complex samples are analyzed.…”

Section: Protein and Peptide Labelingmentioning

confidence: 99%

Quantitative mass spectrometry in proteomics: a critical review

Bantscheff¹,

Schirle²,

Sweetman³

et al. 2007

Anal Bioanal Chem

1,454

1,275

View full text Add to dashboard Cite

The quantification of differences between two or more physiological states of a biological system is among the most important but also most challenging technical tasks in proteomics. In addition to the classical methods of differential protein gel or blot staining by dyes and fluorophores, mass-spectrometry-based quantification methods have gained increasing popularity over the past five years. Most of these methods employ differential stable isotope labeling to create a specific mass tag that can be recognized by a mass spectrometer and at the same time provide the basis for quantification. These mass tags can be introduced into proteins or peptides (i) metabolically, (ii) by chemical means, (iii) enzymatically, or (iv) provided by spiked synthetic peptide standards. In contrast, label-free quantification approaches aim to correlate the mass spectrometric signal of intact proteolytic peptides or the number of peptide sequencing events with the relative or absolute protein quantity directly. In this review, we critically examine the more commonly used quantitative mass spectrometry methods for their individual merits and discuss challenges in arriving at meaningful interpretations of quantitative proteomic data.

show abstract

“…The proposed application of MALDI TOF for AAA contains some advantages over ESI LC/MS/MS or GC/MS: an absence of a need for AA modification; a simplified separation/presentation of sample (e.g., minimal desalting and no LC) with demonstrated quantitative ionization [4], and rapid acquisition of data from 90 plus samples in one "session" for high throughput analysis [10].…”

mentioning

confidence: 99%

MALDI TOF/TOF tandem mass spectrometry as a new tool for amino acid analysis

Gogichaeva

Williams

Alterman

2007

J. Am. Soc. Mass Spectrom.

View full text Add to dashboard Cite

This is the first report of an application of collisionally induced fragmentation of amino acids (AA) and their derivatives by MALDI TOF/TOF tandem mass spectrometry (MS). In this work, we collected the data on high-energy fragmentation reactions of a large group of protonated amino acids and their derivatives with the goal of determining which product ions are analyte specific and if yields of these fragment could be used for quantitative analysis. From 34 different amino acids (20 ␣-amino acids, ␤-amino acids, homocysteine, GABA, and modified AA Met sulfone and sulfoxide, hydroxyproline, etc.) we observed that high yields of the target specific immonium ions and fragmentation patterns are most similar to EI or FAB CID on sector instruments. The major exceptions were two highly basic amino acids, Arg and Orn. It is noted that neither ␤-, ␥-, nor ␦-amino acids produce immonium ions. As might be predicted from high-energy CID work on peptides from the sectors and TOF/TOF, the presence of specific indicator ions in MALDI tandem MS allows distinguishing isomeric and isobaric amino acids. These indicator ions, in combination with careful control of data acquisition, ensure quantitative analysis of amino acids. We believe our data provide strong ince their introduction in the late 1980s, the soft-ionization techniques, electrospray ionization (ESI) and matrix-assisted laser desorption/ ionization (MALDI), have became the major ionization methods for the analysis of biological molecules. While analysis of large biopolymers is successfully performed by both techniques, analysis of low molecular weight (LMW) molecules such as amino acids, pharmaceuticals, hormones, etc. is predominantly performed by ESI mass spectrometry with quadrupole mass analyzers. The major reasons not to use MALDI have been the abundance of matrix ions in the low mass region (100 to 600 u) and the lack of reasonable precursor selection in a MALDI tandem instrument. Also, until recently, MALDI was not considered to be a technique capable of providing robust quantitative data. Current developments in MALDI hardware [1,2] and increased attention paid to sample preparation have changed the situation. A number of recent publications describe application of MALDI TOF for quantitative studies [3][4][5][6][7][8], including favorable comparisons of MALDI TOF with the more traditional ESI LC/MS quantitation schemes [9 -11]. When installed on QqQ instruments, a MALDI source demonstrated good comparability with an ESI source on the same instrument in quantitative analysis of LMW compounds [12].Amino acid analysis (AAA) is one of the areas where ESI LC/MS/MS was successfully applied. ESI LC/ MS/MS has become a standard analytical tool in the analysis of low molecular weight physiological or therapeutic molecules of interest [13][14][15][16].We decided to examine if the combination of highenergy collision and prompt ion detection characteristic for MALDI TOF MS/MS could be applied for AAA. The proposed application of MALDI TOF for AAA contains some advantages o...

show abstract

A Simple Solid Phase Mass Tagging Approach for Quantitative Proteomics

Cited by 43 publications

References 12 publications

Cysteine tagging for MS‐based proteomics

Cysteine tagging for MS‐based proteomics

Quantitative mass spectrometry in proteomics: a critical review

MALDI TOF/TOF tandem mass spectrometry as a new tool for amino acid analysis

Contact Info

Product

Resources

About