Home-made capillary array electrophoresis for high-throughput amino acid analysis

Liu, Kaiying; Wang, Hui; Bai, Jian‐Fei; Wang, Li

doi:10.1016/j.aca.2008.05.062

Cited by 15 publications

(9 citation statements)

References 31 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…). Based on their attractive properties (described in previously published protocols, i.e., synthesis of fluorescent derivatives with high fluorescence quantum yield, compatibility of the excitation wavelength of the derivatized products with commercially available laser sources, stability of the fluorescent adducts, fast reaction rates, and low background signal for NDA and FQ), three different amine‐reactive probes have been selected to label both peptides, two fluorogenic dyes, NDA , and FQ , and one fluorescent dye, TAMRA‐SE . The performance of these dyes, based on the rate of reaction, the degree of substitution, and the detectability of fluorescent products have been compared using CE‐LIF and MS.…”

Section: Introductionmentioning

confidence: 99%

“…Many reports describe also the use of fluorescent dyes such as FITC and rhodamine‐based dyes for LIF detection in the 400–600 nm wavelength range to get near nM LODs. These latter compounds are more reactive than FITC, especially when the dye is activated by the succinimidyl ester group which can react efficiently with unprotonated amines to form a stable amide bond . As an example, 5‐carboxytetramethylrhodamine succinimidyl ester (TAMRA‐SE) labeling of antibodies has been successfully used in SDS‐CGE to obtain LOD as sensitive as silver staining in SDS‐PAGE slab gels .…”

Section: Introductionmentioning

confidence: 99%

See 1 more Smart Citation

Derivatization strategies for CE‐LIF analysis of biomarkers: Toward a clinical diagnostic of familial transthyretin amyloidosis

et al. 2014

View full text Add to dashboard Cite

We report three derivatization strategies for CE analysis with LIF detection (CE-LIF) of two synthetic peptides mimicking the wild and mutated fragments of interest for the diagnosis of familial transthyretin amyloidosis. The precapillary derivatization of the peptides with three optical tags, 5-carboxytetramethylrhodamin succinimidyl ester (TAMRA-SE), naphtalene-2,3-dicarboxyaldehyde (NDA), and 3-(2-furoyl)quinoline-2-carboxyaldehyde (FQ) has been investigated by CE-LIF detection and MS. Results provide evidence that high reaction yields have been reached whereas the multitagging phenomenon has occurred for both NDA and TAMRA-SE labeling procedures. The derivatization and electrokinetic separation of a mixture of the two peptides of interest for the pathology diagnosis (22-aa peptides that differ only from one amino acid) were achieved using both approaches. The highest resolution with a value of 2.5 was obtained with TAMRA-SE labeled derivatives whereas NDA gave the best detection sensitivity (LOD of 2.5 μM). The validation of the developed methods showed a good linearity (R ≥ 0.997) between the peak area of the labeled derivatives and the peptide concentration for both NDA and FQ labeling procedures. The intraday RSDs of A and the migration times were less than 3.8 and 2.2%, respectively.

show abstract

Section: Introductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Derivatization strategies for CE‐LIF analysis of biomarkers: Toward a clinical diagnostic of familial transthyretin amyloidosis

et al. 2014

View full text Add to dashboard Cite

show abstract

“…A different way of improving their MEKC separation was that followed by Liu et al . 44, who used a particular equipment, consisting of a home‐made capillary array system (containing up to 128 capillaries) with confocal rotary scanner for high‐throughput of samples. This experimental setup was applied to the separation of a series ( D / L ‐Ile; ‐Cys and ‐Glu and L ‐Ala; ‐Val; ‐Trp; ‐Cys; ‐Arg; ‐Lys; ‐Glu) of carboxytetramethylrhodamine succinimidyl ester (TAMRA)‐labelled amino acids, which was achieved in less than 10 min using “classical” buffers, i.e .…”

Section: Mekc Of Amino Acids: Methodological Developmentsmentioning

confidence: 99%

MEKC: A powerful tool for the determination of amino acids in a variety of biomatrices

et al. 2009

View full text Add to dashboard Cite

The continued publication from year to year of new MEKC formulations for the analysis of amino acids provides evidence that both CZE and MEKC still have a great power of attraction in this area. The present review intends to cover the literature on MEKC of amino acids from 2007 until present: it has been planned to follow the same format of our previous review (Electrophoresis 2008, 29, 224-236) representing its ideal continuation. In addition to methodological developments, the more recent practical applications of MEKC procedures for the determination of amino acids in different matrices will also be described here as an evidence, once again, of the suitability of this technique on samples of different origin.

show abstract

“…Then a binding constant can be determined in 2 h or less. This speed can be further increased by capillary arrays [44][45][46]. Reported instrumentation allows for a 100-fold throughput [46] but it is expensive to use especially in small laboratories.…”

Section: Calculation Of Binding Constantsmentioning

confidence: 99%

Precision in affinity capillary electrophoresis for drug–protein binding studies

El‐Hady

Kühne

El‐Maali

et al. 2010

Journal of Pharmaceutical and Biomedical Analysis

View full text Add to dashboard Cite

Home-made capillary array electrophoresis for high-throughput amino acid analysis

Cited by 15 publications

References 31 publications

Derivatization strategies for CE‐LIF analysis of biomarkers: Toward a clinical diagnostic of familial transthyretin amyloidosis

Derivatization strategies for CE‐LIF analysis of biomarkers: Toward a clinical diagnostic of familial transthyretin amyloidosis

MEKC: A powerful tool for the determination of amino acids in a variety of biomatrices

Precision in affinity capillary electrophoresis for drug–protein binding studies

Contact Info

Product

Resources

About