High-Performance Liquid Chromatography Analysis in the Synthesis, Characterization, and Reactions of Neoglycopeptides

Morehead, Harvard; McKay, Patrick Zweider; Wetzel, Ronald

doi:10.1016/b978-0-12-335780-9.50025-5

Cited by 3 publications

(7 citation statements)

References 11 publications

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“…The figure shows that the iodoacetylated peptide has disappeared and been replaced by an earlier-eluting peak of similar size. Earlier elution in an aqueous TFA, reversed-phase HPLC system is expected for the addition of carbohydrate to a peptide (4). Closer examination of the peak shows it to be asymmetric, consistent with its being a mixture of related structures.…”

Section: Resultsmentioning

confidence: 77%

“…Of the many chemical methods which have been described, each suffers from one or more limitations. In many conjugation reactions, the amino groups of polypeptides are used as the attachment site, but it is often difficult to control the point of attachment and the extent of modification in a polypeptide containing a number of amino groups (4). Many of the available condensation reactions are relatively inefficient, requiring substantial excesses of carbohydrate (5,6) or polypeptide (7) for significant conversion of a limiting, costly molecule.…”

Section: Introductionmentioning

confidence: 99%

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A novel method for the incorporation of glycoprotein-derived oligosaccharides into neoglycopeptides

Wood¹,

Wetzel²

1992

Bioconjugate Chem.

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We describe a new method for the transfer of carbohydrate moieties to polypeptides in which complex carbohydrate, in the form of glycosyl amino acid, is removed from an available glycoprotein, derivatized, and reacted with a polypeptide via an iodoacetylated alpha-amino group. A family of oligomannose chains, N-linked to the side chain of Asn, was obtained from ovalbumin by pronase digestion and purified as previously described. A reactive sulfhydryl group was specifically placed on these molecules by reaction of 2-iminothiolane with the Asn alpha-amino group. Separately, the alpha-amino group of the peptide GGYR was specifically iodoacetylated by reaction with iodoacetic anhydride at pH 6. Reaction of the thiol-containing carbohydrate with iodoacetylated peptide at pH 8 gave in high yield the corresponding oligomannosyl-peptides, whose structures were confirmed by mass spectrometry. A peptide inhibitor of HIV protease was also oligomannosylated by this procedure. The principle advantage of this method is the efficiency of the reaction even when performed with stoichiometric amounts of the two molecules at low concentration. It should be feasible to extend this chemistry to larger polypeptides.

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Section: Resultsmentioning

confidence: 77%

Section: Introductionmentioning

confidence: 99%

A novel method for the incorporation of glycoprotein-derived oligosaccharides into neoglycopeptides

Wood¹,

Wetzel²

1992

Bioconjugate Chem.

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“…Using the above-described procedure with maltose, we prepared the model spacer sac- (6). The course of the reaction was easily monitored by RP-HPLC.…”

Section: Methodsmentioning

confidence: 99%

“…[R-D-glucopyranosyl(1f4)]--D-glucopyranosylamine (6) to some maleimido-modified peptides. In both cases, very pure products were obtained, upon purification by RP-HPLC.…”

Section: -[S-(triphenylmethyl)mercapto]ethyl]-mentioning

confidence: 99%

A New Method for the Synthesis of Neoglycopeptides

Pb¹,

Olsen²,

Holm³

1998

Bioconjugate Chem.

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A new method for conjugation of small carbohydrates to peptides based on maleimido-thiol chemistry is described. The reducing carbohydrate is reacted with S-trityl-2-mercaptoethylamine in methanol. The resulting Schiff base is then stabilized by acetylation with acetic anhydride to give an S-trityl-protected glycosylamide. Activation of the carbohydrate is effected by brief treatment with trifluoroacetic acid/triisopropylsilane, followed by precipitation in ether. The thiol-functionalized carbohydrate is then reacted with a maleimido-modified peptide to give a neoglycopeptide. The potential of this method was investigated using maltose as the model compound. Furthermore, we prepared five maleimido-modified model peptides. In contrast to some literature reports, we found that the maleimido group is stable to treatment trifluoroacetic acid/triisopropylsilane which was used to cleave the modified peptides from the resin.

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“…Non-specific reductive amination has often been used for linkage of oligosaccharide antigens to protein carriers but the product mixtures are usually not as well characterized as with the lactosylation of N aformyldesacetylthymosin (Morehead et al, 1982(Morehead et al, , 1983.…”

Section: N-linked Neoglycopeptidesmentioning

confidence: 99%

Glycopeptide Synthesis

Meldal¹

1994

Neoglycoconjugates

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High-Performance Liquid Chromatography Analysis in the Synthesis, Characterization, and Reactions of Neoglycopeptides

Cited by 3 publications

References 11 publications

A novel method for the incorporation of glycoprotein-derived oligosaccharides into neoglycopeptides

A novel method for the incorporation of glycoprotein-derived oligosaccharides into neoglycopeptides

A New Method for the Synthesis of Neoglycopeptides

Glycopeptide Synthesis

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