Ion-pair reversed-phase liquid chromatography–electrospray mass spectrometry for the analysis of underivatized small peptides

Pétritis, Konstantinos; Brussaux, Sylvain; Guenu, S.; Elfakir, Claire; Dreux, M.

doi:10.1016/s0021-9673(02)00372-2

Cited by 61 publications

(38 citation statements)

References 62 publications

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“…BGE solutions consisted of 10 mM ammonium acetate -100 mM acetic acid dissolved in a mixture of MeCN and MeOH of varying ratios (between 10 and 90% v/v MeCN in MeOH). The increase in MeCN content induced an increase in the electroosmotic mobility up to 70% v/v MeCN, as previously published [36,37] (data not shown). For the analyte electrophoretic mobilities, two cases can be distinguished: the compounds B2, Z2, A1 and A2, which exhibited relatively constant electrophoretic mobilities throughout the MeCN volume range studied, and the compounds B1 and Z1, which were markedly influenced by the MeCN/ MeOH ratio (Fig.…”

Section: Optimisation Of Nace Separation Conditionssupporting

confidence: 88%

Comparison of CZE, open‐tubular CEC and non‐aqueous CE coupled to electrospray MS for impurity profiling of drugs

et al. 2008

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Open-tubular CEC and non-aqueous CE (NACE) methods were developed for the analysis of six pharmaceutical compounds and their respective process-related impurities, comprising 22 analytes in total with a range of functional groups and lipophilicities. These methods were assessed for orthogonality of analyte separation with respect to existing CZE-ESI-MS and HPLC-ESI-MS methods, in order to complement a generic analytical strategy for impurity profiling of pharmaceutical compounds. Open-tubular CEC, using etched and chemically modified capillaries, induced weak reversed-phase-type interactions between some of the analytes and the bonded phases (0.811

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Section: Optimisation Of Nace Separation Conditionssupporting

confidence: 88%

Comparison of CZE, open‐tubular CEC and non‐aqueous CE coupled to electrospray MS for impurity profiling of drugs

et al. 2008

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“…To analyse the samples by LC-MS, [24] an ion-trap mass spectrometer (Bruker Esquire 3000 plus, Dalton Co., Germany) equipped with an electrospray ionization source was Derivatization procedure: 10 μL of (c) were added to solutions of 20 μL of (a) and 70 μL of (b). After 2 min, 25 μL aliquots were injected into HPLC.…”

Section: Lc-esi-ms Analysismentioning

confidence: 99%

Intermolecular Phosphoryl Transfer of N‐Phosphoryl Amino Acids

et al. 2011

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N-Phosphoryl amino acids (NPAAs) are a novel series of N-terminal-activated amino acids that act as the energy source and phosphoryl donor in intra-and intermolecular phosphoryl transfer to form "high-energy" species, such as acetyl phosphate and aminoacyl phosphates, and in the self-assembled synthesis of polypeptides under mild aqueous conditions. In this work, the chemical reactivity of N-mono(methoxyphosphoryl) glycine as a representative was investigated in detail by using a combination of the stable-isotope-labeling ((15)N) technique, (31)P NMR, ESI-MS/MS and LC-MS. The phosphoryl group of NPAAs can be transferred intermolecularly to the carboxy group of another molecule through intramolecular cyclic pentacoordinate phosphoric-amino acid anhydride intermediates. In addition to C-terminal activation by phosphate anhydride, amino acids can also be self-activated by N-phosphorylation. This information not only provides some interesting clues for understanding the active role of the phosphoryl group in living systems, but also shows that the origin of life might be attributed to the chemical evolution of N-phosphoryl amino acids.National Natural Science Foundation of China (NSFC)[21075103, 20972130, 20805037, 20732004

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“…Different acidic ion-pairing agents are anticipated to create changes in the elution time patterns (the amount of shift and possibly the order) since for the same mobile phase concentration, the hydrophobicity and pKa of the ion-pairing reagent will determine the amount of electrostatic interactions available in the column (assuming that the pH of the mobile phase is determined by the concentration of the ion-pairing reagent in the column) [42,43]. Indeed, for aliphatic acidic ion-pairing reagents, the longer the side chain, the more the column will behave as a dynamic cation-exchanger.…”

Section: Effect Of Different Ion-pairing Agentsmentioning

confidence: 99%

Phosphopeptide elution times in reversed-phase liquid chromatography

Kim

Pétritis

Shen

et al. 2007

Journal of Chromatography A

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Elution time shifts between 33 different peptides and their corresponding phosphopeptides ranging from 4 amino acid residues to 35 amino acids in length were systematically investigated using highresolution reversed-phase liquid chromatography (RPLC)-tandem mass spectrometry (MS/MS) analysis with trifluoroacetic acid as the ion pairing agent. Observed peptide elution time shifts for a single phosphorylation ranged from −5.28 min (for pYVPML) to +0.59 min (for HRDpSGLLDSLGR). Peptides containing a phosphotyrosine residue displayed a significant decrease in elution time following phosphorylation compared to their similar-sized peptides with phosphoserine or phosphothreonine residues. While peptide phosphorylation generally led to a decrease in the observed elution time, five peptides displayed increased elution times as a result of phosphorylation. For large peptides (= 18 amino acids), the elution time shifts due to single phosphorylation were limited (ranging between −0.48 min and +0.03 min), while the elution time shifts for small peptides (< 18 amino acids) were characterized by a larger deviation (ranging between −5.28 min and +0.59 min). The predictive capability for the observed RPLC elution time change due to phosphorylation has been suggested, which will aid in assigning confident phosphopeptide identifications and their subsequent confirmation.

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Ion-pair reversed-phase liquid chromatography–electrospray mass spectrometry for the analysis of underivatized small peptides

Cited by 61 publications

References 62 publications

Comparison of CZE, open‐tubular CEC and non‐aqueous CE coupled to electrospray MS for impurity profiling of drugs

Comparison of CZE, open‐tubular CEC and non‐aqueous CE coupled to electrospray MS for impurity profiling of drugs

Intermolecular Phosphoryl Transfer of N‐Phosphoryl Amino Acids

Phosphopeptide elution times in reversed-phase liquid chromatography

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