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Cover Picture: Glyco‐Scan: Varying Glycosylation in the Sequence of the Peptide Hormone PYY3‐36 and Its Effect on Receptor Selectivity (ChemBioChem 3/2010)
Author(s) -
Pedersen Søren L.,
Steentoft Catharina,
Vrang Niels,
Jensen Knud J.
Publication year - 2010
Publication title -
chembiochem
Language(s) - English
Resource type - Reports
SCImago Journal Rank - 1.05
H-Index - 126
eISSN - 1439-7633
pISSN - 1439-4227
DOI - 10.1002/cbic.201090005
Subject(s) - peptide , pentapeptide repeat , receptor , glycosylation , chemistry , selectivity , biochemistry , biology , catalysis
The cover picture shows the concept of a glyco‐scan of a peptide, as demonstrated for the hormone PYY3‐36. PYY3‐36 has been implicated in food intake regulation, and novel peptide analogues with high Y2‐receptor‐subtype selectivity and potency have potential as drugs for the treatment of obesity. It has been hypothesized that PYY3‐36 associates with the plasma membrane prior to receptor activation so that the amphipathic α‐helix of PYY3‐36 can guide the C‐terminal pentapeptide into the correct conformation for receptor activation. On p. 366 ff., N. Vrang, K. J. Jensen et al. show how the introduction and systematic variation of glycosylation in the peptide PYY3‐36 can be used to „scan“ a peptide analogous to an Ala scan. This demonstrated that glycosylation of PYY3‐36 is well tolerated in several positions and even improves the Y‐receptor selectivity. The glyco‐scan concept, as systematically demonstrated here, has the potential for wide applicability. (Cover design Jesper Cairo Westergaard.)