Modification of triantennary glycopeptide into probes for the asialoglycoprotein receptor of hepatocytes

Kevin G Rice; Yuan C Lee

doi:10.1016/S0021-9258(17)44769-7

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Modification of triantennary glycopeptide into probes for the asialoglycoprotein receptor of hepatocytes

Journal article

Open access

Peer reviewed

Modification of triantennary glycopeptide into probes for the asialoglycoprotein receptor of hepatocytes

Kevin G Rice and Yuan C Lee

The Journal of biological chemistry, Vol.265(30), pp.18423-18428

10/25/1990

DOI: 10.1016/S0021-9258(17)44769-7

PMID: 2211710

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Abstract

Triantennary glycopeptide was oxidized with galactose oxidase to convert the -CH2OH group on terminal galactose residues to the aldehyde group (oxo-form). Kinetic profiling by reverse phase high performance liquid chromatography allowed termination of the reaction when intermediate mono-oxo- and di-oxo-triantennary glycopeptides had been produced. The mixture of the oxo-glycopeptides was derivatized with 2,4-dinitrophenylhydrazine for efficient separation, and each isomeric triantennary hydrazone was separated by reverse phase high performance liquid chromatography. The purified hydrazones were reverted to three original isomeric mono-oxo- and di-oxo-glycopeptides, and a single tri-oxo-glycopeptide. Each of these isomers was characterized by proton NMR by a downfield shift in the anomeric signals of 6-oxo-Gal residue(s). The functionalized glycopeptides were successively modified with dansyl and naphthyl groups through the 6-oxo-Gal residue and the amino terminus of the peptide to prepare three isomeric glycopeptide probes suitable for conformation studies by fluorescence energy transfer measurements. Alternatively, glycopeptides were derivatized by attaching t-butyloxycarbonyl-L-tyrosine to the amino terminus of the peptide, and reductive amination of the 6-oxo-Gal residue, provided three isomeric triantennary photoaffinity probes which allow photolyzable groups to be attached to the newly introduced 6-amino-Gal residue.

Affinity Labels

Asialoglycoprotein Receptor

Asialoglycoproteins - metabolism

Carbohydrate Sequence

Chromatography, High Pressure Liquid

Fluorescent Dyes

Galactose Oxidase - pharmacology

Glycopeptides - chemical synthesis

Glycopeptides - chemistry

Glycopeptides - metabolism

Magnetic Resonance Spectroscopy

Molecular Sequence Data

Oxidation-Reduction

Receptors, Immunologic - metabolism

Details

Title: Subtitle: Modification of triantennary glycopeptide into probes for the asialoglycoprotein receptor of hepatocytes
Creators: Kevin G Rice - Johns Hopkins University
Yuan C Lee
Resource Type: Journal article
Publication Details: The Journal of biological chemistry, Vol.265(30), pp.18423-18428
DOI: 10.1016/S0021-9258(17)44769-7
PMID: 2211710
NLM abbreviation: J Biol Chem
ISSN: 0021-9258
eISSN: 1083-351X
Grant note: DK09970 / NIDDK NIH HHS GM 13013-01 BI-4 / NIGMS NIH HHS
Language: English
Date published: 10/25/1990
Academic Unit: Pharmaceutical Sciences and Experimental Therapeutics; Craniofacial Anomalies Research Center; Medicinal and Natural Products Chemistry
Record Identifier: 9984365894602771

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