Artículos de revistas
Use of commercial anion-exchange resins as solid support for peptide synthesis and affinity chromatography
Fecha
2003-07-01Registro en:
Analytical Biochemistry. San Diego: Academic Press Inc. Elsevier B.V., v. 318, n. 1, p. 39-46, 2003.
0003-2697
10.1016/S0003-2697(03)00196-9
WOS:000183495900006
9424346762460416
0000-0002-4767-0904
Autor
Universidade Federal de São Paulo (UNIFESP)
Universidade Estadual Paulista (Unesp)
Institución
Resumen
This report demonstrates that due to the presence of residual reactive sites in their matrices, classical diethylaminoethyl-attaching commercial anion-exchanger resins such as DEAE-MacroPrep and DEAE-Sephadex A50 supports can be used for peptide synthesis. Moreover, due to the high stability of the peptide-resin bond in the final cleavage treatments, desired peptidyl-resins free of side-chain protecting groups, which enables them to be further used as solid support for affinity chromatography, can be obtained. To demonstrate this potentiality, a fragment corresponding to the antigenic and immunodominant epitope of sporozoites of the Plasmodium falciparum malaria parasite was synthesized in these traditional resins and antibody molecules generated against the peptide sequence were successfully retained in these peptidyl supports. Due to the maintenance of their original anion-exchange capacities, the present findings open the unique possibility of applying, simultaneously, dual anion-exchange and affinity procedures for purification of a variety of macromolecules. (C) 2003 Elsevier B.V. (USA). All rights reserved.