| Title | Glycosylation of pramlintide: Synthetic glycopeptides that display in vitro and in vivo activities as amylin receptor agonists |
| Publication Type | Journal Article |
| Year of Publication | 2013 |
| Authors | Tomabechi, Y., Krippner G., Rendle P.M., Squire M.A., and Fairbanks A.J. |
| Journal | Chemistry - A European Journal |
| Volume | 19 |
| Issue | 45 |
| Pagination | 15084 - 15088 |
| Date Published | 2013 |
| ISSN | 09476539 (ISSN) |
| Keywords | amylin, 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 |
| Abstract | 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. © 2013 WILEY-VCH Verlag GmbH & Co. KGaA, Weinheim. |
| URL | http://www.scopus.com/inward/record.url?eid=2-s2.0-84886640647&partnerID=40&md5=0426e8b649822d85d85db22f646923c3 |
| DOI | 10.1002/chem.201303303 |
