Strategies for the highly efficient synthesis of erythropoietin N-glycopeptide hydrazides.
Autor: | Hessefort M; Bioorganic Chemistry, University of Bayreuth, Universitätsstraße 30, Bayreuth, 95447, Germany., Hessefort H; Bioorganic Chemistry, University of Bayreuth, Universitätsstraße 30, Bayreuth, 95447, Germany., Seeleithner S; Bioorganic Chemistry, University of Bayreuth, Universitätsstraße 30, Bayreuth, 95447, Germany., Gross A; Bioorganic Chemistry, University of Bayreuth, Universitätsstraße 30, Bayreuth, 95447, Germany., Lott M; Bioorganic Chemistry, University of Bayreuth, Universitätsstraße 30, Bayreuth, 95447, Germany., Rau D; Bioorganic Chemistry, University of Bayreuth, Universitätsstraße 30, Bayreuth, 95447, Germany., Kern L; Bioorganic Chemistry, University of Bayreuth, Universitätsstraße 30, Bayreuth, 95447, Germany., Unverzagt C; Bioorganic Chemistry, University of Bayreuth, Universitätsstraße 30, Bayreuth, 95447, Germany. |
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Jazyk: | angličtina |
Zdroj: | Journal of peptide science : an official publication of the European Peptide Society [J Pept Sci] 2021 Jan; Vol. 27 (1), pp. e3283. Date of Electronic Publication: 2020 Sep 03. |
DOI: | 10.1002/psc.3283 |
Abstrakt: | A convergent synthesis for erythropoietin (EPO) 1-28 N-glycopeptide hydrazides was developed. In this approach, EPO 1-28 peptides were synthesized on the solid phase and converted to C-terminal hydrazides after cleavage from the resin. After selective deprotection of the Asp24 side chain, the desired glycosylamine was coupled by pseudoproline-assisted Lansbury aspartylation. Although the initial yields of the EPO 1-28 glycopeptides were satisfactory, they could be markedly improved by increasing the purity of the peptide using a reversed-phase high-performance liquid chromatography (RP-HPLC) purification of the protected peptide. (© 2020 European Peptide Society and John Wiley & Sons, Ltd.) |
Databáze: | MEDLINE |
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