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Glycosylation of Pramlintide: Synthetic Glycopeptides that Display In Vitro and In Vivo Activities as Amylin Receptor Agonists
Author(s) -
Tomabechi Yusuke,
Krippner Guy,
Rendle Phillip M.,
Squire Marie A.,
Fairbanks Antony J.
Publication year - 2013
Publication title -
chemistry – a european journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.687
H-Index - 242
eISSN - 1521-3765
pISSN - 0947-6539
DOI - 10.1002/chem.201303303
Subject(s) - glycan , glycosylation , glycopeptide , amylin , in vivo , in vitro , chemistry , biochemistry , receptor , computational biology , glycoprotein , computer science , biology , endocrinology , microbiology and biotechnology , insulin , islet , antibiotics
Sweet 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.