Capillary electrophoresis laser-induced fluorescence for screening combinatorial peptide libraries in assays of botulinum neurotoxin A

Laing, T D; Marenco, Armando J.; Moore, Diana M.; Moore, Graham J.; Mah, David; Lee, William

doi:10.1016/j.jchromb.2006.06.011

Cited by 15 publications

(14 citation statements)

References 20 publications

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“…CE was used to characterize acid phosphatase from Spirodella oligorrhiza [221], polyanion-protein complexes [222], dynamics of proteinase activation [223], proteins from Spirulina platensis microalga [224,225], F5cys-MP-PEG(2000)-DPSE protein-lipopolymer [226], basic proteins immobilized on polymer particles [227], RNA interference with sialidase [228], and combitorial peptide libraries in an assay of botulinum neurotoxin A [229].…”

Section: Studying Behavior Of Proteinsmentioning

confidence: 99%

Capillary electrophoresis of proteins 2005–2007

Dolnı́k¹

2007

Electrophoresis

152

106

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This review article with 239 references describes recent developments in capillary electrophoresis of proteins, and covers the two years since the previous review (V. Dolník, Electrophoresis 2006, 27, 126-141) through spring 2007. It includes topics related to CE of proteins, such as sample pretreatment, wall coatings, improving separation, various forms of detection, and special electrophoretic techniques including ACE, CIEF, capillary ITP, and CEC. The paper describes applications of CE to analysis of proteins in real-world samples including human body fluids, food and agricultural samples, protein pharmaceuticals and recombinant protein preparations.

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Section: Studying Behavior Of Proteinsmentioning

confidence: 99%

Capillary electrophoresis of proteins 2005–2007

Dolnı́k¹

2007

Electrophoresis

152

106

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“…In classical PAGE, SDS eliminates differences of the intrinsic mobility of the proteins by the formation of complexes with the same charge-to-mass ratio [5][6][7][8][9][10][11][12][13][14][15][16][17][18][19][20]. Normally, such complexes cannot be resolved when free in solution, but can be separated according to their size upon application of sieving matrices.…”

Section: Introductionmentioning

confidence: 99%

Effect of detergent on electromigration of proteins: CE of very low density lipoprotein receptor modules and viral proteins

2007

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The different electrophoretic behavior of the members of two groups of proteins with respect to the absence or presence of detergent additives in the BGE was explored. Recombinant soluble concatemers of repeat 3 of the very low density lipoprotein (VLDL)-receptor fused at their N-terminus to maltose-binding protein (MBP) exhibited different electrophoretic mobilities in borate buffer (pH 8.3) in the absence and in the presence of dodecyl-PEG ether (D-PEG). This enabled the separation of the receptor fragments from MBP after enzymatic cleavage. In the presence of SDS, the mobilities of all proteins approached the same values with increase in detergent concentrations. In contrast, viral capsid proteins of a human rhinovirus (HRV) exhibited different migration in the presence of the additive. For the receptor proteins, extreme apparent high plate numbers were observed when the SDS concentration in the sample and the separation buffer differed. This effect might be erroneously interpreted as a high efficiency. However, it is due to the conductivity boundaries caused by the sample and leads to a total loss of separation.

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“…Two CE modes, CZE and CMEKC, were applied to the screening of combinatorial peptide libraries for their inhibitory activites to botulinum neurotoxin serotype A, a proteolytic enzyme that induces muscle paralysis [219]. The peptide products in this enzyme assay were labeled with 3-(4-carboxy-benzoyl)-2-quinoline-carboxaldehyde (CBQCA) and separated by CZE or MEKC with LIF detection (Ar ion laser, excitation/emission at 488/520 nm).…”

Section: Monitoring Of Chemical and Enzymatical Reactions And Physicamentioning

confidence: 99%

Recent developments in CE and CEC of peptides

Kašička

2007

Electrophoresis

118

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The article brings a comprehensive survey of recent developments and applications of high-performance capillary electromigration methods, zone electrophoresis, ITP, IEF, affinity electrophoresis, EKC, and electrochromatography, to analysis, preparation, and physicochemical characterization of peptides. New approaches to the theoretical description and experimental verification of electromigration behavior of peptides and to methodology of their separations, such as sample preparation, adsorption suppression, and detection, are presented. Novel developments in individual CE and CEC modes are shown and several types of their applications to peptide analysis are presented: conventional qualitative and quantitative analysis, purity control, determination in biomatrices, monitoring of chemical and enzymatical reactions and physical changes, amino acid and sequence analysis, and peptide mapping of proteins. Some examples of micropreparative peptide separations are given and capabilities of CE and CEC techniques to provide important physicochemical characteristics of peptides are demonstrated.

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Capillary electrophoresis laser-induced fluorescence for screening combinatorial peptide libraries in assays of botulinum neurotoxin A

Cited by 15 publications

References 20 publications

Capillary electrophoresis of proteins 2005–2007

Capillary electrophoresis of proteins 2005–2007

Effect of detergent on electromigration of proteins: CE of very low density lipoprotein receptor modules and viral proteins

Recent developments in CE and CEC of peptides

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