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TitleGlycosylation of pramlintide: Synthetic glycopeptides that display in vitro and in vivo activities as amylin receptor agonists
Publication TypeJournal Article
Year of Publication2013
AuthorsTomabechi, Y., Krippner G., Rendle P.M., Squire M.A., and Fairbanks A.J.
JournalChemistry - A European Journal
Pagination15084 - 15088
Date Published2013
ISSN09476539 (ISSN)
Keywordsamylin, article, Asn residues, Blood glucose, carbohydrate, Carbohydrates, chemical structure, chemistry, diabetes, diabetes mellitus, Enzymatic glycosylation, enzyme, Enzymes, Esterification, glycopeptide, Glycopeptides, Glycosylated, glycosylation, human, Humans, Islet Amyloid Polypeptide, Medical problems, Molecular Structure, N-glycan structures, Peptides, pramlintide, Solid phase peptide synthesis
AbstractSweet medicine: Glycosylated analogues of pramlintide, in which specific Asn residues bear extended N-glycan structures, may be accessed by a combination of solid-phase peptide synthesis and highly efficient enzymatic glycosylation (see scheme; ENGases=endo-β-N-acetylglucosaminidases). Glycopeptides display both in vitro and in vivo activity as amylin receptor agonists and effect 'smoothing' of blood glucose. © 2013 WILEY-VCH Verlag GmbH & Co. KGaA, Weinheim.

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