Use of commercial anion-exchange resins as solid support for peptide synthesis and affinity chromatography


Autoria(s): Nakaie, C. R.; Lanzer, D. A.; Malavolta, L.; Cilli, Eduardo Maffud; Rodrigues, M. M.
Contribuinte(s)

Universidade Estadual Paulista (UNESP)

Data(s)

20/05/2014

20/05/2014

01/07/2003

Resumo

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.

Formato

39-46

Identificador

http://dx.doi.org/10.1016/S0003-2697(03)00196-9

Analytical Biochemistry. San Diego: Academic Press Inc. Elsevier B.V., v. 318, n. 1, p. 39-46, 2003.

0003-2697

http://hdl.handle.net/11449/35215

10.1016/S0003-2697(03)00196-9

WOS:000183495900006

Idioma(s)

eng

Publicador

Elsevier B.V.

Relação

Analytical Biochemistry

Direitos

closedAccess

Palavras-Chave #peptide #resin #polymer #ion-exchange chromatography #affinity chromatography
Tipo

info:eu-repo/semantics/article