Application of amino acid analysis using hydrophilic interaction liquid chromatography coupled with isotope dilution mass spectrometry for peptide and protein quantification

Kato, Megumi; Kato, Hisashi; Eyama, Sakae; Takatsu, Akiko

doi:10.1016/j.jchromb.2009.07.027

Cited by 69 publications

(46 citation statements)

References 21 publications

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“…All these IHI values could be compared with the elution order of amino acids separated by ZIC-HILIC reported by Kato et al [33]:…”

Section: Hilic-ms Separationmentioning

confidence: 99%

“…Hydrophilic interaction chromatography (HILIC) is becoming increasingly popular [27][28][29][30] and has been successfully used for the separation of peptides [31,32] and of amino acids [33,34]. The growing interest in HILIC is partly due to its high solvent compatibility with MS in the electrospray ionization (ESI) mode [35,36].…”

Section: Introductionmentioning

confidence: 99%

“…The growing interest in HILIC is partly due to its high solvent compatibility with MS in the electrospray ionization (ESI) mode [35,36]. One of the major fields currently under investigation is the use of HILIC as a separation tool for proteomic applications [33,[36][37][38], but it is also studied for use in mixed-mode [39][40][41] and two-dimensional liquid chromatography (2D LC) [42][43][44][45].…”

Section: Introductionmentioning

confidence: 99%

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Hydrophilic properties as a new contribution for computer-aided identification of short peptides in complex mixtures

et al. 2012

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A new method to predict elementary amino acid (AA) composition of peptides (molar mass <1,000 g/mol) is described. This procedure is based on a computer-aided method using three combined analyses-reversed phase liquid chromatography (RPLC), hydrophilic interaction chromatography (HILIC) and capillary electrophoresis coupled with mass spectrometry-and using a software calculating all possible amino acid combinations from the mass of any given peptide. The complementarity between HILIC and RPLC was demonstrated. Peptide retention prediction in HILIC was successfully modelled, and the achieved prediction accuracy was as high as r²=0.97. This mathematical model, based on amino acid retention contributions and peptide length, provided the information about peptide hydrophilicity that was not redundant with its hydrophobicity. Correlations between respectively the hydrophobicity coefficients and RPLC retention time, hydrophilicity and HILIC retention time, and electrophoretic mobility and migration time were used for ranking all potential AA combinations corresponding to the given mass. The essential contribution of HILIC in this identification strategy and the need to combine the three models to significantly increase identification capabilities were both shown. Applied to an 18-standard peptide mixture, the identification procedure enabled the actual AA combination determination of the 14 di- to pentapeptides, in addition to an over 98 % reduction of possible combination numbers for the four hexapeptides. This procedure was then applied to the identification of 24 unknown peptides in a rapeseed protein hydrolysate. The effective AA composition was found for ten peptides, whereas for the 14 other peptides, the number of possible combinations was reduced by over 95 % thanks to the association of the three analyses. Finally, as a result of the information provided by the analytical techniques about peptides present in the mixture, the proposed method could become a highly valuable tool to recover bioactive peptides from undefined protein hydrolysates.

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“…All these IHI values could be compared with the elution order of amino acids separated by ZIC-HILIC reported by Kato et al [33]:…”

Section: Hilic-ms Separationmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

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Hydrophilic properties as a new contribution for computer-aided identification of short peptides in complex mixtures

et al. 2012

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“…6 In addition, 17 kinds of proteinogenic amino acids are targeted for amino acid composition analysis or accurate quantification of protein/peptide. [7][8][9][10][11][12][13][14][15] In these methods, the constituent amino acids released from the original protein/ peptide through hydrolysis are quantified.…”

Section: Introductionmentioning

confidence: 99%

Development of High-purity Certified Reference Materials for 17 Proteinogenic Amino Acids by Traceable Titration Methods

et al. 2015

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“…The hydrolyzed free amino acid has traditionally been separated by reversed phase column with ion-pairing reagents such as tridecafluoroheptanoic acid and nonafluoropentanoic acid to ensure the separation, 1,2 and recently, also by hydrophilic interaction liquid chromatography (HILIC). 3,4 However, both reversed phase chromatography and HILIC can separate only a limited number of amino acids, and these applications are having difficulties with the maintenance of the separation over the repeated injections and with the reproducibility of quantitation for hydrophilic amino acids. An alternative method to address the above points, precolumn derivatization of amino acids for LC-MS analysis using a reversed phase column, has been developed.…”

Section: Introductionmentioning

confidence: 99%

Traceable Amino Acid Analyses of Proteins and Peptides by Isotope-Dilution Mass Spectrometry Using Precolumn Derivatization Reagent

et al. 2010

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Application of amino acid analysis using hydrophilic interaction liquid chromatography coupled with isotope dilution mass spectrometry for peptide and protein quantification

Cited by 69 publications

References 21 publications

Hydrophilic properties as a new contribution for computer-aided identification of short peptides in complex mixtures

Hydrophilic properties as a new contribution for computer-aided identification of short peptides in complex mixtures

Development of High-purity Certified Reference Materials for 17 Proteinogenic Amino Acids by Traceable Titration Methods

Traceable Amino Acid Analyses of Proteins and Peptides by Isotope-Dilution Mass Spectrometry Using Precolumn Derivatization Reagent

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