Long-chained gemini surfactants for semipermanent wall coatings in capillary electrophoresis of proteins.
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.
Liu
Qian
Q
College of Chemistry & Chemical Engineering, Hunan University, Changsha, P. R. China.
Yuan
Jinbin
J
Li
Yanqing
Y
Yao
Shouzhuo
S
D019075:Electrophoresis, Capillary / Q000379:methods*; D006863:Hydrogen-Ion Concentration; D011506:Proteins / Q000032:analysis*; D013501:Surface-Active Agents / Q000737:chemistry*
D011506:Proteins; D013501:Surface-Active Agents