Improved properties of the non-covalent coating with N,N-didodecyl-N, N-dimethylammonium bromide for the separation of basic proteins by capillary electrophoresis with acidic buffers in 25μm capillaries

Mohabbati, Sheila; Westerlund, Douglas

doi:10.1016/j.chroma.2006.03.125

Cited by 28 publications

(20 citation statements)

References 47 publications

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“…Therefore, the influence of PAMAMs as additives on separation performance varies with buffer pH. On the other hand, buffers of wide pH range have been employed for high performance separation of proteins by CE/CEC, from extremely acidic [15], mild acidic [16][17][18][19][20] to neutral [12,[21][22][23][24], mild alkaline [25,26] and extremely alkaline [27]. Therefore, examining the properties of PAMAM dendrimers as additives in different pHs is helpful in extending their potential applications in protein analysis.…”

Section: Introductionmentioning

confidence: 98%

Cationic poly(amidoamine) dendrimers as additives for capillary electroseparation and detection of proteins

et al. 2011

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We examine the influence of cationic poly(amidoamine) (PAMAM) dendrimers on capillary electroseparation-UV analysis of proteins. PAMAMs adsorbing to the capillary surface suppressed the wall-adsorption of proteins; meanwhile, PAMAMs added to the buffer exhibited selectivity toward proteins. Presence of 3 x 10⁻⁴ g/mL PAMAM generation one (G 1.0) in 30 mM phosphate, at pH 2.6, rendered significant enhancement in separation efficiency; the merged peaks of myoglobin and trypsin inhibitor were separated. Moreover, the protein-dendrimer interactions changed the inherent UV absorbance profiles of proteins. UV-Vis study showed that the absorbance of cytochrome C and transferrin increased at the detection wavelength of 214 nm; their detection sensitivity enhanced by 2.44 and 2.01-folds, respectively, with addition of 5 x 10⁻⁴ g/mL PAMAM G 1.0.

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Section: Introductionmentioning

confidence: 98%

Cationic poly(amidoamine) dendrimers as additives for capillary electroseparation and detection of proteins

et al. 2011

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“…Generally, in the systems of fully dynamic zwitterionic coating, the surfactants must be present in the buffer, which alters the protein mobility and leads to the decrease of the detector signal, and also makes coating incompatible with electrospray-mass spectrometric detection. Some of the cationic double-chained surfactants, e.g., didodecyldimethylammonium bromide (DDAB), which are adsorbed to the capillary inner surface so strongly that their addition in the running buffer is not needed, are only suitable for the separation of basic proteins [25]. Recently, Jennifer et al developed a phospholipid DLPCbased semi-permanent dynamic coating to separate both basic and acidic proteins with efficiencies up to 1 million plates/m.…”

Section: Introductionmentioning

confidence: 99%

Simultaneous separation of basic and acidic proteins using 1‐butyl‐3‐methylimidazolium‐based ion liquid as dynamic coating and background electrolyte in capillary electrophoresis

Wei

et al. 2008

Electrophoresis

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1-Butyl-3-methylimidazolium tetrafluoroborate ionic liquids (1B-3MI-TFB ILs) were employed as a coating material and BGE in CE for simultaneous separation of basic and acidic proteins such as lysozyme, cytochrome C, ribonuclease A, albumin, and alpha-lactalbumin. 1B-3MI-TFB ILs effectively reversed the surface charges on the capillary inner surface, preventing the adsorption of positively charged proteins onto the silica surface, as well as associated with proteins, thus benefiting the separation efficiencies and reproducibility. Consequently, simultaneous baseline separation of five proteins was achieved within 14 min by using 10 mM of 1B-3MI-TFB ILs as dynamic coating and the only running electrolyte at the voltage of +20 kV. The proposed coating technique is simple, less time-consuming, reproducible, and also stable enough for proteins separation without the need of additives. Symmetrical peaks with efficiencies up to 670,000 plates/m were obtained. Recoveries of proteins with RSD (for migration times) of 0.23-0.42% (run-to-run) and 2.5-3.8% (day-to-day) were achieved, respectively. The applicability of the proposed method in proteins separation was evaluated by the separation of egg white samples.

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“…The cationic double-chained surfactant, dimethyldidodecylammonium bromide, was one of the most intensively investigated surfactant-based semi-permanent coatings for analysis of basic proteins [11][12][13][14]. The positively charged bilayer surface produced a highly reproducible reversed (anodic) EOF, which was highly effective in separating cationic proteins.…”

Section: Introductionmentioning

confidence: 99%

Sphingomyelins as semi‐permanent capillary coatings for protein separations in CE and off‐line analysis with MALDI‐MS

Jurčić

Yeung

2009

Electrophoresis

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Phosphatidylcholine (PC) is one of the major phospholipids that make up the biological cell membrane. It was previously reported to form capillary inner wall coatings for CE. The zwitterionic head group of PC produced a neutral net-charged bilayer, which was found effective in preventing wall adsorption of both cationic and anionic proteins [J. M. Cunliffe et al. Anal. Chem. 2002, 74, 776-783]. Another major membrane phospholipid that possesses a zwitterionic head group is sphingomyelin (SM). In this work, the novel characterization of SM on its effectiveness in capillary coating formation for CE separations of proteins and peptides was presented. Similar properties were observed between PC and SM, including their effects on the EOF, peak efficiencies, and migration time reproducibilities. SM appeared to be more readily soluble in aqueous solutions, and it was found equally effective as PC in facilitating protein separation. The main difference observed was their performances in delivering a peptide mixture for off-line analysis with MALDI-MS. Superior sample recovery was evident from the capillary coated with SM compared with that with PC. The number of peptides identified from a 1 ng/microL myglobin tryptic digest sample increased from 5 to 16 (42 and 69%, respectively in protein sequence coverage).

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Improved properties of the non-covalent coating with N,N-didodecyl-N, N-dimethylammonium bromide for the separation of basic proteins by capillary electrophoresis with acidic buffers in 25μm capillaries

Cited by 28 publications

References 47 publications

Cationic poly(amidoamine) dendrimers as additives for capillary electroseparation and detection of proteins

Cationic poly(amidoamine) dendrimers as additives for capillary electroseparation and detection of proteins

Simultaneous separation of basic and acidic proteins using 1‐butyl‐3‐methylimidazolium‐based ion liquid as dynamic coating and background electrolyte in capillary electrophoresis

Sphingomyelins as semi‐permanent capillary coatings for protein separations in CE and off‐line analysis with MALDI‐MS

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