A rapid and robust method for amino acid quantification using a simple N-hydroxysuccinimide ester derivatization and liquid chromatography-ion mobility-mass spectrometry

Domenick, Taylor M; Jones, Austin L.; Kemperman, Robin H. J.; Yost, Richard A.

doi:10.1007/s00216-022-03993-w

Cited by 4 publications

(4 citation statements)

References 29 publications

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“…One such candidate method is the employment of correction functions based on a set of internal standards spiked into all samples to be used for multiple correction functions or for internal calibrations [35,36]. While the use of natural internal standards limits the number of compounds that can be spiked, SIL-based internal standardization are ideal candidates for application to LC-IM-MS methods by exploiting the alignment of isotopologues in both LC and IM dimensions [18,37,38]. Due to their frequent use as internal standards for quantitative purposes, the potential of increasing the scope of this approach to include an internal correction for CCS N2 determination was also considered here for the first time for steroid analysis.…”

Section: Evaluation Of Internal Correction Using Stable Isotope Label...mentioning

confidence: 99%

Critical evaluation of the role of external calibration strategies for IM-MS

et al. 2022

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The major benefits of integrating ion mobility (IM) into LC–MS methods for small molecules are the additional separation dimension and especially the use of IM-derived collision cross sections (CCS) as an additional ion-specific identification parameter. Several large CCS databases are now available, but outliers in experimental interplatform IM-MS comparisons are identified as a critical issue for routine use of CCS databases for identity confirmation. We postulate that different routine external calibration strategies applied for traveling wave (TWIM-MS) in comparison to drift tube (DTIM-MS) and trapped ion mobility (TIM-MS) instruments is a critical factor affecting interplatform comparability. In this study, different external calibration approaches for IM-MS were experimentally evaluated for 87 steroids, for which TWCCSN2, DTCCSN2 and TIMCCSN2 are available. New reference CCSN2 values for commercially available and class-specific calibrant sets were established using DTIM-MS and the benefit of using consolidated reference values on comparability of CCSN2 values assessed. Furthermore, use of a new internal correction strategy based on stable isotope labelled (SIL) internal standards was shown to have potential for reducing systematic error in routine methods. After reducing bias for CCSN2 between different platforms using new reference values (95% of TWCCSN2 values fell within 1.29% of DTCCSN2 and 1.12% of TIMCCSN2 values, respectively), remaining outliers could be confidently classified and further studied using DFT calculations and CCSN2 predictions. Despite large uncertainties for in silico CCSN2 predictions, discrepancies in observed CCSN2 values across different IM-MS platforms as well as non-uniform arrival time distributions could be partly rationalized.

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Section: Evaluation Of Internal Correction Using Stable Isotope Label...mentioning

confidence: 99%

Critical evaluation of the role of external calibration strategies for IM-MS

et al. 2022

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“…The interference of the matrix and the existence of isomers limit the quantitative analysis of biological metabolites . High-resolution IM-MS based on SLIM can realize rapid and repeatable quantitative analysis .…”

Section: Applications Of Im-ms For the Separation And Characterizatio...mentioning

confidence: 99%

“…97 The interference of the matrix and the existence of isomers limit the quantitative analysis of biological metabolites. 98 Highresolution IM-MS based on SLIM can realize rapid and repeatable quantitative analysis. 99 Among the existing instru-ments, TIMS and FAIMS are most commonly used for quantitative analysis.…”

Section: And Characterization Of Small Moleculesmentioning

confidence: 99%

Ion Mobility Mass Spectrometry for the Separation and Characterization of Small Molecules

et al. 2023

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“…For instance, p-N,N,N-trimethylammonioanilyl N′-hydroxysuccinimidyl carbamate iodide achieved subfemtomole to attomole levels of AAs detection [95]. Other examples (see Table 2 and Figure 4) [95][96][97][98][99][100][101][102][103][104][105] are dibenzyl ethoxymethylene malonate and benzyl ethyl ethoxymethylene malonate [105] as well as 4-dimethylaminobenzoylamido acetic acid N-hydroxysuccinimide ester [106] and dimethy-laminophenacyl bromide [107]. By synthesizing 3-aminopyridyl-N-hydroxysuccinimidyl carbamate (APDS) reagent, Shimbo et al [97] could measure over 105 amino compounds in rat plasma and quantify 22 AAs within 10 min.…”

Section: Hplc Tandem Msmentioning

confidence: 99%

Overview of chromatographic and electrophoretic methods for the determination of branched‐chain amino acids

Yin

Adams

Schepdael

2023

J of Separation Science

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The significance of branched‐chain amino acids in diseases was clearly shown over the years. This review aims to describe the available techniques for their analytical determination. The article provides examples of the use of various analytical methods. The methods are divided into two categories: derivatization and non‐derivatization approaches. Separation is achieved through different chromatography or capillary electrophoresis techniques and can be combined with different detectors such as flame ionization, ultraviolet, fluorescence, and mass spectrometry. It compares the application of various derivatization reagents or detection as such for different detectors.

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A rapid and robust method for amino acid quantification using a simple N-hydroxysuccinimide ester derivatization and liquid chromatography-ion mobility-mass spectrometry

Cited by 4 publications

References 29 publications

Critical evaluation of the role of external calibration strategies for IM-MS

Critical evaluation of the role of external calibration strategies for IM-MS

Ion Mobility Mass Spectrometry for the Separation and Characterization of Small Molecules

Overview of chromatographic and electrophoretic methods for the determination of branched‐chain amino acids

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