Strategies for the highly efficient synthesis of erythropoietin N‐glycopeptide hydrazides. (3rd September 2020)

• Record Type: Journal Article
• Authors: Hessefort, Markus; Hessefort, Hendrik; Seeleithner, Simone; Gross, Angelina; Lott, Marie; Rau, David; Kern, Laura; Unverzagt, Carlo
• Is Part Of: Journal of peptide science. Volume 27:Number 1(2021)
• Page Start: n/a
• Page End: n/a
• Publication Date: 2020-09-03
• Subjects: glycopeptide -- HPLC -- purification -- solid‐phase peptide synthesis; Peptides -- Periodicals; Peptides -- Periodicals; 572.65
• DOI: 10.1002/psc.3283
• Languages: English
• ISSNs: 1075-2617

Abstract

Abstract : 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. Abstract : The purification of the EPO 1‐28 hydrazide A by nonconventional HPLC methods was found to be crucial for high yields of glycopeptide B via pseudoproline‐assisted Lansbury aspartylation.