2-Aminobenzamide and 2-Aminobenzoic Acid as New MALDI Matrices Inducing Radical Mediated In-Source Decay of Peptides and Proteins

Smargiasso, Nicolas; Quinton, Loïc; Pauw, Edwin De

doi:10.1007/s13361-011-0307-5

Cited by 37 publications

(40 citation statements)

References 30 publications

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“…16) Recently, a number of matrices have been developed to increase the performance of MALDI-ISD for peptides and proteins. In particular, 1,5-diaminonaphtalene (1,5-DAN) 17) and 2-aminobenzoic acid (2-AA) 18) were reported to efficiently induce the MALDI-ISD of peptides and proteins. MALDI is well suited for use with axial time-of-flight (TOF) mass spectrometers.…”

Section: )mentioning

confidence: 99%

5-Nitrosalicylic Acid as a Novel Matrix for In-Source Decay in Matrix-Assisted Laser Desorption/Ionization Mass Spectrometry

Asakawa

2013

Mass Spectrometry

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The matrix-assisted laser desorption/ionization in-source decay (MALDI-ISD) of peptides and glycans was studied using an oxidizing chemical, 5-nitrosalicylic acid (5-NSA) as the matrix. The use of 5-NSA for the MALDI-ISD of peptides and glycans promoted fragmentation pathways involving "hydrogen-deficient" radical precursors. Hydrogen abstraction from peptides resulted in the production of a "hydrogen-deficient" peptide radical that contained a radical site on the amide nitrogen in the peptide backbone with subsequent radical-induced cleavage at the C α -C bonds. Cleavage at the C α -C bond leads to the production of an a• /x fragment pair and the radical a • ions then undergo further hydrogen abstraction to form a ions after C α -C bond cleavage. Since the Pro residue does not contain a nitrogen-centered radical site, C α -C bond cleavage does not occur at this site. Alternatively, the specific cleavage of CO−N bonds leads to a b• /y fragment pair at Xxx−Pro which occurs via hydrogen abstraction from the C α −H in the Pro residue. In contrast, "hydrogen-deficient" glycan radicals were generated by hydrogen abstraction from hydroxyl groups in glycans. Both glycosidic and cross-ring cleavages occurred as the result of the degradation of "hydrogen-deficient" glycan radicals. Cross-ring cleavage ions are potentially useful in linkage analysis, one of the most critical steps in the characterization of glycans. Moreover, isobaric glycans could be distinguished by structure specific ISD ions, and the molar ratio of glycan isomers in a mixture can be estimated from their fragment ions abundance ratios. MALDI-ISD with 5-NSA could be a useful method for the sequencing of peptides including the location of post-translational modifications, identification and semi-quantitative analysis of mixtures of glycan isomers.

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Section: )mentioning

confidence: 99%

5-Nitrosalicylic Acid as a Novel Matrix for In-Source Decay in Matrix-Assisted Laser Desorption/Ionization Mass Spectrometry

Asakawa

2013

Mass Spectrometry

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“…However, this matrix remains less efficient than the 1,5-DAN matrix and rather difficult to use (low solubility) but possesses the advantage of being non-carcinogenic. Very recently, two additional molecules were shown to induce radical-induced fragmentation of peptides and proteins -2-aminobenzoic acid (2-AA, also known as anthranilic acid) and 2-aminobenzamide (2-AB) [21].…”

Section: Isd Mechanismsmentioning

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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“…The identity of proteins was further confirmed by using MALDI in-source decay (ISD) fragmentation. ISD fragmentation occurs in the ion source of the MALDI mass spectrometer and can lead to the formation of c-and z-fragment ions, but also a-, b-, x-, and y-fragment ions depending on the MALDI matrix used (35)(36)(37)(38)(39)(40)(41)(42)(43)(44)(45). This approach has already been used for peptide and protein identification either in solution (38,46,47) or in situ (48)(49)(50)(51).…”

Section: Resultsmentioning

confidence: 99%

MALDI mass spectrometry imaging analysis of pituitary adenomas for near-real-time tumor delineation

Calligaris

Feldman

Norton

et al. 2015

Proc. Natl. Acad. Sci. U.S.A.

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We present a proof of concept study designed to support the clinical development of mass spectrometry imaging (MSI) for the detection of pituitary tumors during surgery. We analyzed by matrix-assisted laser desorption/ionization (MALDI) MSI six nonpathological (NP) human pituitary glands and 45 hormone secreting and nonsecreting (NS) human pituitary adenomas. We show that the distribution of pituitary hormones such as prolactin (PRL), growth hormone (GH), adrenocorticotropic hormone (ACTH), and thyroid stimulating hormone (TSH) in both normal and tumor tissues can be assessed by using this approach. The presence of most of the pituitary hormones was confirmed by using MS/MS and pseudo-MS/MS methods, and subtyping of pituitary adenomas was performed by using principal component analysis (PCA) and support vector machine (SVM). Our proof of concept study demonstrates that MALDI MSI could be used to directly detect excessive hormonal production from functional pituitary adenomas and generally classify pituitary adenomas by using statistical and machine learning analyses. The tissue characterization can be completed in fewer than 30 min and could therefore be applied for the nearreal-time detection and delineation of pituitary tumors for intraoperative surgical decision-making. mass spectrometry imaging | pituitary | molecular pathology | intrasurgical diagnosis | in-source decay

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2-Aminobenzamide and 2-Aminobenzoic Acid as New MALDI Matrices Inducing Radical Mediated In-Source Decay of Peptides and Proteins

Cited by 37 publications

References 30 publications

5-Nitrosalicylic Acid as a Novel Matrix for In-Source Decay in Matrix-Assisted Laser Desorption/Ionization Mass Spectrometry

5-Nitrosalicylic Acid as a Novel Matrix for In-Source Decay in Matrix-Assisted Laser Desorption/Ionization Mass Spectrometry

MALDI In-Source Decay, from Sequencing to Imaging

MALDI mass spectrometry imaging analysis of pituitary adenomas for near-real-time tumor delineation

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