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.
Highlights
Erythropoietin (EPO) is a cytokine needed for the homeostasis of erythrocytes
We found that the efficient synthesis of EPO 1-28 glycopeptides requires a high purity of both the glycosylamine and the selectively deprotected peptide
As shown before,[22] EPO 1-28 glycopeptides can be synthesized on the solid phase in a straightforward manner
Summary
Erythropoietin (EPO) is a cytokine needed for the homeostasis of erythrocytes. Therapeutic EPO is expressed recombinantly in Chinese hamster ovary (CHO) cells and used mainly to treat anemic patients suffering from renal failure or cancer.[1]. KEYWORDS glycopeptide, HPLC, purification, solid-phase peptide synthesis The convergent synthesis of N-glycopeptides following the aspartylation method developed by Lansbury[20] involves the coupling of a glycosylamine to an aspartyl side chain of a protected peptide.
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