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  • Title: Long-chained gemini surfactants for semipermanent wall coatings in capillary electrophoresis of proteins.
    Author: Liu Q, Yuan J, Li Y, Yao S.
    Journal: Electrophoresis; 2008 Feb; 29(4):871-9. PubMed ID: 18297646.
    Abstract:
    In this paper, we presented the first example of using gemini surfactants as semipermanent coatings in CE for protein separation. These coatings are based on the self-assembly of a series of cationic gemini surfactants, alkanediyl-alpha,omega-bis(dimethylalkylammonium bromide) (m-s-m), on the capillary wall. The coatings can keep stable for a long time without surfactant in the buffer, e.g., after the surfactants were removed from the buffer, the reversed EOF only decreased by 3.6 and 3.9% for 18-2-18 and 16-2-16 coatings over 60 min under continuous electrophoretic conditions. The coating stability increased with the alkyl chain length m. The double long chains of geminis (m > or = 14) yielded a good coating stability; meanwhile, the spacer group acted as an EOF modifier. Thus, this bifunctional surfactant coating provided a new buffer-independent method for EOF control. For 18-s-18 series, the best coating stability and largest EOF were obtained at s = 10. Ranging s from 3 to 10 yielded a linear fine-tuning of EOF and thereby allowed the adjustment of the protein apparent mobility. Highly efficient separation (>500 000 plates/m) was achieved with all the 18-s-18 coatings. Excellent run-to-run and day-to-day reproducibility (RSD of migration time </=0.7 and 4.3% for run-to-run and day-to-day assays, respectively) and fine recoveries (97.5-100.1%) of the protein samples indicated that the gemini semipermanent coatings were quite effective for the wall adsorption suppression of proteins.
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