Simultaneous analysis of enantiomeric composition of amino acids and N‐acetyl‐amino acids by enantioselective chromatography

Yu, Yi‐Ping; Wu, Shih‐Hsiung

doi:10.1002/chir.1024

Cited by 13 publications

(9 citation statements)

References 29 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…A number of papers have reported the successful use of teicoplanin stationary phases for the LC separation of amino acid enantiomers 21–26. Teicoplanin is a macrocyclic glycopeptide with numerous chiral centers 21.…”

Section: Introductionmentioning

confidence: 99%

Analysis of native amino acid and peptide enantiomers by high‐performance liquid chromatography/atmospheric pressure chemical ionization mass spectrometry

Desai

Armstrong

2004

J. Mass Spectrom.

View full text Add to dashboard Cite

High-performance liquid chromatography (HPLC) coupled to atmospheric pressure chemical ionization (APCI) mass spectrometry was used for the separation and detection of amino acid and peptide enantiomers. With detection limits as low as 250 pg, 25 amino acids enantiomers were baseline resolved on a Chirobiotic T chiral stationary phase. APCI demonstrated an order of magnitude better sensitivity over electrospray ionization (ESI) for free amino acids and low molecular mass peptides at the high LC flow-rates necessary for rapid analysis. As the peptide chain length increased (peptides with M(r) > or = 300 Da), however, ESI proved to be the more ideal atmospheric pressure ionization source. A mobile phase consisting of 1% (w/w) ammonium trifluoroacetate in methanol and 0.1% (w/w) formic acid in water increased the sensitivity of the APCI method significantly. A step gradient was then used to separate simultaneously all 19 native protein amino acid enantiomers in less than 20 min using extracted ion chromatograms.

show abstract

Section: Introductionmentioning

confidence: 99%

Analysis of native amino acid and peptide enantiomers by high‐performance liquid chromatography/atmospheric pressure chemical ionization mass spectrometry

Desai

Armstrong

2004

J. Mass Spectrom.

View full text Add to dashboard Cite

show abstract

“…Current approaches to the determination of D ‐amino acids include enzymatic,18 chromatographic19–22 and immunohistochemical23 methods. Of these methods, high‐performance liquid chromatography (HPLC)19 and capillary electrophoresis (CE)24 are often preferred, especially when combined with laser‐induced fluorescence (LIF) detection to improve selectivity and sensitivity.…”

Section: Introductionmentioning

confidence: 99%

Kinetic method for the simultaneous chiral analysis of different amino acids in mixtures

Tao

Cooks

2003

J. Mass Spectrom.

View full text Add to dashboard Cite

The kinetic method has been extended to enantiomeric excess (ee) determinations on amino acids present in mixtures. Singly charged trimeric clusters [Cu(II)(ref*)(2)(A(m)) - H](+) are readily generated by electrospraying solutions containing Cu(II), a chiral reference ligand (ref*), and the amino acids (analytes A(m), m = 1-3). A trimeric cluster ion for each amino acid is individually mass-selected and then collisionally activated to cause dissociation by competitive loss of either the reference ligand or the analyte. For each analyte in the mixture, as shown from separate experiments, the logarithm of the ratio of the fragment abundances for the complex containing one enantiomer of this analyte expressed relative to that for the fragments of the corresponding complex containing the other enantiomer is linearly related to the enantiomeric composition of the amino acid. Formation and dissociation of each trimeric complex ion are shown to occur independently of the presence of other analytes. Chiral selectivity appears to be an intrinsic property and the chiral selectivity R(chiral(m)) measured from the mixture of analytes is equal to R(chiral) measured for the pure analyte. The sensitive nature of the methodology and the linear relationship between the logarithm of the fragment ion abundance ratio and the optical purity, characteristic of the kinetic method, allow the determination of chiral impurities of less than 2% ee in individual compounds present in mixtures by simply recording the ratios of fragment ion abundances in a tandem mass spectrum.

show abstract

“…In order to evaluate the acylase activity in selected KAPs, we developed an analytical method to carry out the monitoring progress of the reaction; the typical colorimetric (ninhydrin) procedure [21] was difficult to reproduce even for the calibration curve, this method resulted to be too sensitive to the time and temperature of the reaction, which led to great variations in the results. In consequence, we decided to use HPLC, since it is an easier to handle and more reproducible method.…”

Section: Resultsmentioning

confidence: 99%

Comparative Study on the N-acylase Activity of Mammalian Kidney Acetone Powders (KAP’s)

et al. 2017

View full text Add to dashboard Cite

The N-acylase activity and enantioselectivity of mammalian kidney acetone powders (KAP’s) or their enzyme extract was demonstrated on (rac)-N-acetylmethionine; used as reference substrate. It was showed hydrolysis exclusively on the (S)-enantiomer. The biocatalyzed reaction allowed us, to categorize the KAPs regarding the animal source, sheep, pig, calf, bovine, dog and guinea pig as fast biocatalysts reaching equilibrium in around 4 to 5 h; and rat, mouse and hamster were slower biocatalysts, since they did it in around 24 h. In most of the reactions the kidney crude preparations gave a better conversion than the enzyme extract, this fact demonstrated that the longer stirring during the reaction in an aqueous medium, allowed a greater dissolution of the enzyme. These readily available and inexpensive crude biocatalysts have a great potential application in organic synthesis.

show abstract

Simultaneous analysis of enantiomeric composition of amino acids and N‐acetyl‐amino acids by enantioselective chromatography

Cited by 13 publications

References 29 publications

Analysis of native amino acid and peptide enantiomers by high‐performance liquid chromatography/atmospheric pressure chemical ionization mass spectrometry

Analysis of native amino acid and peptide enantiomers by high‐performance liquid chromatography/atmospheric pressure chemical ionization mass spectrometry

Kinetic method for the simultaneous chiral analysis of different amino acids in mixtures

Comparative Study on the N-acylase Activity of Mammalian Kidney Acetone Powders (KAP’s)

Contact Info

Product

Resources

About