0162367 - UIACH-O 20020018 RIV DE eng J - Článek v odborném periodiku
Cretich, M. - Šťastná, Miroslava - Chrambach, A. - Chiari, M.
Decreased protein peak asymmetry and width due to static capillary coating with hydrophilic derivatives of polydimethylacrylamide.
Electrophoresis. Roč. 23, č. 14 (2002), s. 2274-2278. ISSN 0173-0835. E-ISSN 1522-2683
Výzkumný záměr: CEZ:AV0Z4031919
Klíčová slova: capillary coating * capillary zone electrophoresis
Kód oboru RIV: CB - Analytická chemie, separace
Impakt faktor: 4.325, rok: 2002

Protein CZE peaks in the EPDMA-coated capillaries exhibited a peak asymmetry similar to that obtained in capillaries with "covalent static" coating of polyacrylamide, suggesting a similar degree of adsorption of the protein onto the coating. Instability of such coating at very low ionic strength and its stripping from the capillary in the presence of SDS also indicated a hydrophilic bonding of EPDMA to the silanol surface of the capillary, while its stripping in the CZE of "carboxylate-modified" polystyrene suggested a competition between carboxylate and EPDMA for the hydrophilic bonds to silanol. To test those propositions, a number of EPDMA-derived coating agents with increased hydrophilicity were syntesized. Of a number of the hydrophilic coating agents tested, only two exhibited for representative proteins a decreased peak asymmetry and width while the stability of the suppresion of EOF, and the stability of mobility in consecutive CZE runs was reduced relative to EPDMA. Coating agents which were more hydrophilic than those two provided no stable static coating.**rene suggested a competition between carboxylate and EPDMA for the hydrophilic bonds to silanol. To test those propositions, a number of EPDMA-derived coating agents with increased hydrophilicity were syntesized. Of a number of the hydrophilic coating
Trvalý link: http://hdl.handle.net/11104/0059685