Comparative time-course study of aminoacyl- and dipeptidyl-resin hydrolysis

• Autor(a) principal: Jubilut,Guita N.
• Data de Publicação: 1997
• Outros Autores: Marchetto,Reinaldo, Cilli,Eduardo M., Oliveira,Eliandre, Miranda,Antonio, Tominaga,Mineko, Nakaiee,Clóvis R.
• Tipo de documento: Artigo
• Idioma: eng
• Título da fonte: Journal of the Brazilian Chemical Society (Online)
• Texto Completo: http://old.scielo.br/scielo.php?script=sci_arttext&pid=S0103-50531997000100012
• topic: peptide hydrolysis; resin; acid hydrolysis; amino acid analysis; acyl-resin hydrolysis; solid phase peptide synthesis

The classic hydrolysis procedure for quantification of resin-bound aminoacyl and peptidyl groups with 12 N HCl: propionic acid was reevaluated by studying the influence of the nature of the resin and the resin-bound group. Their stability during acid hydrolysis was dependent on the C-terminal amino acid, and the order of acid stability was Phe > Val > Gly. Otherwise, the dipeptides Ala-Gly, Ala-Val, and Ala-Phe displayed enhanced rates of hydrolysis of the resin if compared with their parent aminoacyl groups. Amongthe resins assayed, the order of acid stability was: benzhydrylamine-resin>p-methylbenzhydrylamine-resin ≅4-(oxymethyl)-phenylacetamidomethyl-resin > chloromethyl-copolymer of styrene-1%-divinylbenzene. Important for peptide synthesis method, the findings demonstrate that longer hydrolysis times than previously recommended in the literature (1 h at 130 °C and 15 min at 160 °C for peptides attached to the chloromethyl-copolymer of styrene-1%-divinylbenzene) are necessary for the quantitative acid-catalyzed cleavage of some resin-bound groups. The observed broad range of hydrolysis time varied from less than 1 h to about 100 h.