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The Glycosylation of AGP and Its Associations with the Binding to Methadone

Behan, Jennifer L.; Cruickshank, Yvonne E.; Matthews-Smith, Gerri; Bruce, Malcolm; Smith, Kevin D.

Authors

Jennifer L. Behan

Yvonne E. Cruickshank

Malcolm Bruce

Kevin D. Smith



Abstract

Methadone remains the most common form of pharmacological therapy for opioid dependence; however, there is a lack of
explanation for the reports of its relatively low success rate in achieving complete abstinence. One hypothesis is that in vivo binding
of methadone to the plasma glycoprotein alpha-1-acid glycoprotein (AGP), to a degree dependent on the molecular structure,
may render the drug inactive. This study sought to determine whether alterations present in the glycosylation pattern of AGP in
patients undergoing various stages of methadone therapy (titration < two weeks, harm reduction < one year, long-term > one and
a half years) could affect the affinity of the glycoprotein to bind methadone. The composition of AGP glycosylation was determined
using high pH anion exchange chromatography (HPAEC) and intrinsic fluorescence analysed to determine the extent of binding to
methadone. The monosaccharides galactose and N-acetyl-glucosamine were elevated in all methadone treatment groups indicating
alterations in AGP glycosylation. AGP from all patients receiving methadone therapy exhibited a greater degree of binding than the
normal population. This suggests that analysing the glycosylation of AGP in patients receiving methadone may aid in determining
whether the therapy is likely to be effective.

Journal Article Type Article
Publication Date 2013
Deposit Date Mar 10, 2015
Publicly Available Date Mar 10, 2015
Print ISSN 2314-6133
Electronic ISSN 2314-6141
Publisher Hindawi
Peer Reviewed Peer Reviewed
Volume 2013
Pages 1-7
DOI https://doi.org/10.1155/2013/108902
Keywords General Biochemistry, Genetics and Molecular Biology; General Immunology and Microbiology; General Medicine
Public URL http://researchrepository.napier.ac.uk/id/eprint/7662
Publisher URL http://dx.doi.org/10.1155/2013/108902
Contract Date Mar 10, 2015

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