Comparison of liquid chromatography with tandem mass spectrometry and ion-exchange chromatography by post-column ninhydrin derivatization for amino acid monitoring

Šmon, Andraž; Čuk, Vanja; Brecelj, Jernej; Murko, Simona; Grošelj, Urh; Tanšek, Mojca Žerjav; Battelino, Tadej; Lampret, Barbka Repič

doi:10.1016/j.cca.2019.05.007

Cited by 24 publications

(26 citation statements)

References 10 publications

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“…18–20 Derivatization can improve chromatographic separation and mass spectrometric properties of small m/z species, for example, glycine, proline and alanine, measurement of which presents a specific challenge for LC-MS-based methods. 21,22 Disadvantages include poor reproducibility of the derivative yield, variable derivatization efficiency of different amino acids and the instability of the derivatives. 23,24 Ion pair reagents negate the need for derivatization and facilitate good chromatographic separation.…”

Section: Discussionmentioning

confidence: 99%

“…23,24 Ion pair reagents negate the need for derivatization and facilitate good chromatographic separation. 20–26 However, they are prone to retention time instability and reagents may foul the LC components, ion source and mass spectrometer causing signal suppression in subsequent analysis and diminished column performance. This lack of robustness and efficiency limits routine utility and, more recently, methods have been described which negate the need for derivatization or ion pair reagents.…”

Section: Discussionmentioning

confidence: 99%

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Challenging the status quo: A comparison of ion exchange chromatography with liquid chromatography–mass spectrometry and liquid chromatography–tandem mass spectrometry methods for the measurement of amino acids in human plasma

et al. 2020

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Background Plasma amino acid analysis is key to the diagnosis and monitoring of inherited disorders of amino acid synthesis, catabolism and transport. Ion exchange chromatography (IEC) is widely accepted as the gold standard method of analysis, but with the introduction of liquid chromatography tandem mass spectrometry (LC-MS/MS) and liquid chromatography mass spectrometry (LC-MS) methods, this should now be questioned. Methods The analytical performance of three commercially available reagent kits, Waters AccQ Tag™ ULTRA LC-MS, SpOtOn Amino Acids LC-MS/MS and Chromsystems MassChrom® Amino Acid Analysis LC-MS/MS, were evaluated and compared with Biochrom Physiological Amino Acids ion exchange chromatography. Correlation with IEC was assessed by Passing-Bablok regression, concordance correlation coefficients (CCC) and Bland-Altman analysis for 21 common amino acids. Calculation of the total error from imprecision and bias was also used to benchmark performance. Results The MassChrom® and SpOtOn kits demonstrated acceptable inter-batch imprecision (CV < 10%) and accuracy (mean bias < 10%), whereas the AccQ Tag™ ULTRA kit did not. Good correlation (CCC > 0.95) with Biochrom IEC was demonstrated for 10/21 analytes in both the MassChrom® and SpOtOn kits and 6/21 in the AccQ Tag™ ULTRA kit. Conclusions The LC-MS assay demonstrated variable analytical performance and correlated poorly with ion exchange chromatography. Both LC-MS/MS assays demonstrated comparable analytical performance and reasonable correlation with ion exchange chromatography. They also confer practical advantages which cannot be realized by ion exchange chromatography, superior specificity and significantly faster analysis time, suggesting that ion exchange chromatography should no longer be described as the gold standard method for plasma amino acid analysis.

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Section: Discussionmentioning

confidence: 99%

Section: Discussionmentioning

confidence: 99%

Challenging the status quo: A comparison of ion exchange chromatography with liquid chromatography–mass spectrometry and liquid chromatography–tandem mass spectrometry methods for the measurement of amino acids in human plasma

et al. 2020

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“…The major disadvantage is that it is a time-consuming method (usually 2-3 h per sample) that requires high sample volumes (>200 µL). In addition, detecting interfering compounds that react with ninhydrin and cannot be determined by spectrophotometric detection generates problems [65,66]. The LC-MS/MS technique has become a compelling tool because of its better selectivity and shorter analysis times compared to IEC.…”

Section: Routine Methods For Detection Of Aas Proteins and Peptidesmentioning

confidence: 99%

Amino Acids, Peptides, and Proteins: Implications for Nanotechnological Applications in Biosensing and Drug/Gene Delivery

Laraib

Arshad

et al. 2021

Nanomaterials

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Over various scientific fields in biochemistry, amino acids have been highlighted in research works. Protein, peptide- and amino acid-based drug delivery systems have proficiently transformed nanotechnology via immense flexibility in their features for attaching various drug molecules and biodegradable polymers. In this regard, novel nanostructures including carbon nanotubes, electrospun carbon nanofibers, gold nanoislands, and metal-based nanoparticles have been introduced as nanosensors for accurate detection of these organic compounds. These nanostructures can bind the biological receptor to the sensor surface and increase the surface area of the working electrode, significantly enhancing the biosensor performance. Interestingly, protein-based nanocarriers have also emerged as useful drug and gene delivery platforms. This is important since, despite recent advancements, there are still biological barriers and other obstacles limiting gene and drug delivery efficacy. Currently available strategies for gene therapy are not cost-effective, and they do not deliver the genetic cargo effectively to target sites. With rapid advancements in nanotechnology, novel gene delivery systems are introduced as nonviral vectors such as protein, peptide, and amino acid-based nanostructures. These nano-based delivery platforms can be tailored into functional transformation using proteins and peptides ligands based nanocarriers, usually overexpressed in the specified diseases. The purpose of this review is to shed light on traditional and nanotechnology-based methods to detect amino acids, peptides, and proteins. Furthermore, new insights into the potential of amino protein-based nanoassemblies for targeted drug delivery or gene transfer are presented.

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“… determination of rimantadine (antiviral drug) from human urine samples with o ‐phthalaldehyde and N‐ acetyl‐cysteine for HPLC with fluorescence detection (Zacharis & Tzanavaras, 2020); amino‐acid monitoring in plasma samples from patients with phenylketonuria by means of ion‐exchange liquid chromatography with tandem mass spectrometry and post‐column derivatization with ninhydrin (Smon et al, 2019); post‐column derivatization of neurotoxin domoic acid with 4‐chloro‐7‐nitrobenzo‐2‐oxa‐1,3‐diazole (NBD‐Cl) in order to avoid the interference of fluorescent 4‐hydroxy‐7‐nitrobenzo‐2‐oxa‐1,3‐diazole, which is the hydrolysis product of NBD‐Cl (Maroulis, Monemvasios, Vardaka, & Rigas, 2008); post‐column derivatization reaction of oxaliplatin with N , N‐ diethyldithiocarbamate for HPLC–UV determination in complex biological samples (Ehrsson & Wallin, 2003); photochemical degradation of barbiturates using post‐column ultra‐violet irradiation for their HPLC–UV detection in forensic biological samples (Garcia‐Borregon, Lores, & Cela, 2000); oxidative dimerization of morphine to the fluorescent compound pseudo‐morphine by post‐column derivatization reaction with potassium hexacyanoferrate (III) (Emara, 1998). …”

Section: Post‐column Derivatizationmentioning

confidence: 99%

Derivatization procedures and their analytical performances for HPLC determination in bioanalysis

David

Moldoveanu

Galaon

2020

Biomedical Chromatography

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Derivatization, or chemical structure modification, is often used in bioanalysis performed by liquid chromatography technique in order to enhance detectability or to improve the chromatographic performance for the target analytes. The derivatization process is discussed according to the analytical procedure used to achieve the reaction between the reagent and the target compounds (containing hydroxyl, thiol, amino, carbonyl and carboxyl as the main functional groups involved in derivatization). Important procedures for derivatization used in bioanalysis are in situ or based on extraction processes (liquid-liquid, solid-phase and related techniques) applied to the biomatrix. In the review, chiral, isotope-labeling, hydrophobicity-tailored and post-column derivatizations are also included, based on representative publications in the literature during the last two decades. Examples of derivatization reagents and brief reaction conditions are included, together with some bioanalytical applications and performances (chromatographic conditions, detection limit, stability and sample biomatrix).

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Comparison of liquid chromatography with tandem mass spectrometry and ion-exchange chromatography by post-column ninhydrin derivatization for amino acid monitoring

Cited by 24 publications

References 10 publications

Challenging the status quo: A comparison of ion exchange chromatography with liquid chromatography–mass spectrometry and liquid chromatography–tandem mass spectrometry methods for the measurement of amino acids in human plasma

Challenging the status quo: A comparison of ion exchange chromatography with liquid chromatography–mass spectrometry and liquid chromatography–tandem mass spectrometry methods for the measurement of amino acids in human plasma

Amino Acids, Peptides, and Proteins: Implications for Nanotechnological Applications in Biosensing and Drug/Gene Delivery

Derivatization procedures and their analytical performances for HPLC determination in bioanalysis

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