Abstract
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.
Talk to us
Join us for a 30 min session where you can share your feedback and ask us any queries you have
Schedule a callDisclaimer: All third-party content on this website/platform is and will remain the property of their respective owners and is provided on "as is" basis without any warranties, express or implied. Use of third-party content does not indicate any affiliation, sponsorship with or endorsement by them. Any references to third-party content is to identify the corresponding services and shall be considered fair use under The CopyrightLaw.
