Chiral separations using dextran and bovine serum albumin as run buffer additives in affinity capillary electrophoresis

Sun, Peng; Wu, Nian; Barker, Geoffrey E.; Hartwick, Richard A.

doi:10.1016/0021-9673(93)80431-7

Cited by 72 publications

(23 citation statements)

References 24 publications

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“…In other work it has been shown that the addition of dextran will alter the migration of HSA and bovine serum albumin, while having a much smaller effect on the mobility of smaller solutes [32][33][34].…”

Section: Use Of Dextran To Modify Mobilitiesmentioning

confidence: 99%

Identification of drug-binding sites on human serum albumin using affinity capillary electrophoresis and chemically modified proteins as buffer additives

2002

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A technique based on affinity capillary electrophoresis (ACE) and chemically modified proteins was used to screen the binding sites of various drugs on human serum albumin (HSA). This involved using HSA as a buffer additive, following the site-selective modification of this protein at two residues (tryptophan 214 or tyrosine 411) located in its major binding regions. The migration times of four compounds (warfarin, ibuprofen, suprofen and flurbiprofen) were measured in the presence of normal or modified HSA. These times were then compared and the mobility shifts observed with the modified proteins were used to identify the binding regions of each injected solute on HSA. Items considered in optimizing this assay included the concentration of protein placed into the running buffer, the reagents used to modify HSA, and the use of dextran as a secondary additive to adjust protein mobility. The results of this method showed good agreement with those of previous reports. The advantages and disadvantages of this approach are examined, as well as its possible extension to other solutes.

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Section: Use Of Dextran To Modify Mobilitiesmentioning

confidence: 99%

Identification of drug-binding sites on human serum albumin using affinity capillary electrophoresis and chemically modified proteins as buffer additives

2002

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“…Barker and colleagues [21] used bovine serum albumin as buffer additive in uncoated and coated capillaries. Sun et al [22] developed a method combining bovine serum albumin and dextran as buffer additives that was further improved by the use of a bovine serum albumin dextran polymer [23]. The simultaneous separation of the diastereomers of folinic acid and its major me- 2004 WILEY-VCH Verlag GmbH & Co. KGaA, Weinheim tabolite 5-methyltetrahydrofolic acid was achieved using g-cyclodextrin (g-CD) as chiral selector in sodium phosphate buffer, pH 7.1 or pH 9.1 [24].…”

Section: Levofolinic Acid (2s)-2-[[4-[[[(6s)mentioning

confidence: 97%

Development and validation of a robust capillary electrophoresis method for impurity profiling of calcium levofolinate including the (6R,2'S)‐diastereomer using statistical experimental design

et al. 2004

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A chiral capillary electrophoresis assay for the simultaneous determination of the optical purity and of related substances of calcium levofolinate has been developed and validated. Using 2,6-dimethyl-beta-cyclodextrin as chiral selector at a concentration of 20 mg/mL, the method was optimized using a full factorial design with four factors including pH and concentration of the background electrolyte, column temperature and separation voltage. Optimized conditions were a 40 mM sodium tetraborate buffer, pH 9.9, a capillary temperature of 16 degrees C, and an applied voltage of 21 kV. Methotrexate was used as internal standard to compensate for injection errors and fluctuations of the migration times. A multiple linear regression model was also used to test the robustness of the method. Validation was performed with respect to specificity, linearity, range, limit of quantification and detection, precision, and accuracy. The assay allowed the detection and determination of related substances including the diastereomeric (6R,2'S)-impurity of levofolinic acid at the 0.1% level, the identification threshold of impurities for orally administered drugs for human use defined by the International Conference on Harmonization guidelines as well as the European Pharmacopoeia.

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“…Examples have included the addition of the proteins avidin [83,118], flavoprotein [119] and bovine serum albumin (BSA) [120] to the BGE as chiral selectors. The data obtained from these investigations are summarized in Table 1.…”

Section: Miscellaneous Chiral Selectors For the Resolution Of 2-apasmentioning

confidence: 99%

Enantiomeric resolution of 2‐arylpropionic acid nonsteroidal anti‐inflammatory drugs by capillary electrophoresis: Methods and applications

Patel¹,

Hanna-Brown²,

Hadley³

et al. 2004

Electrophoresis

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The 2-arylpropionic acids (2-APAs) are an important group of nonsteroidal anti-inflammatory drugs. These agents, the majority of which are available as racemates, exhibit stereoselectivity in both their action and disposition. Developments in stereoselective separation science methodology, mainly chromatographic, have facilitated an evaluation of the pharmacological properties of the individual enantiomers of these drugs and contributed to our understanding of both their mode(s) of action and disposition. While a number of electrophoretic techniques, including capillary electrophoresis, capillary electrochromatography and isotachophoresis, have been applied to the stereoselective resolution and stereospecific analysis of these agents using a variety of chiral selectors, e.g., cyclodextrins, oligosaccharides, macrocyclic antibiotics, and proteins, the number of published applications in pharmaceutical and biomedical analysis remains relatively limited. However, the utility of electrophoretic techniques for stereospecific analysis may be illustrated using the 2-APAs as typical examples of chiral acidic pharmaceuticals. Applications include: determination of enantiomeric composition following biosynthetic stereoselective hydrolysis; examination of both achiral and chiral impurity profiles in bulk drugs and formulated products; determination of enantiomeric impurities in both bulk drugs and formulated products; examination of configurational stability following stress testing of formulated products; determination of enantiomeric composition and metabolite profile in biological fluids following administration of the racemates and individual enantiomers. It may be anticipated that future exploitation of electrophoretic approaches to the stereospecific analysis of these agents will result in further contributions to our understanding of their stereoselective biological properties and therapeutic use.

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Chiral separations using dextran and bovine serum albumin as run buffer additives in affinity capillary electrophoresis

Cited by 72 publications

References 24 publications

Identification of drug-binding sites on human serum albumin using affinity capillary electrophoresis and chemically modified proteins as buffer additives

Identification of drug-binding sites on human serum albumin using affinity capillary electrophoresis and chemically modified proteins as buffer additives

Development and validation of a robust capillary electrophoresis method for impurity profiling of calcium levofolinate including the (6R,2'S)‐diastereomer using statistical experimental design

Enantiomeric resolution of 2‐arylpropionic acid nonsteroidal anti‐inflammatory drugs by capillary electrophoresis: Methods and applications

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