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Cover Picture: Peptide Architecture: Adding an α‐Helix to the PYY Lysine Side Chain Provides Nanomolar Binding and Body‐Weight‐Lowering Effects (ChemMedChem 4/2010)
Author(s) -
Pedersen Søren L.,
Sasikumar Pottayil G.,
Vrang Niels,
Jensen Knud J.
Publication year - 2010
Publication title -
chemmedchem
Language(s) - English
Resource type - Reports
SCImago Journal Rank - 0.817
H-Index - 100
eISSN - 1860-7187
pISSN - 1860-7179
DOI - 10.1002/cmdc.201090010
Subject(s) - peptide , helix (gastropod) , chemistry , receptor , cover (algebra) , side chain , amphiphile , stereochemistry , n terminus , crystallography , biophysics , biochemistry , peptide sequence , biology , engineering , gene , ecology , organic chemistry , snail , copolymer , polymer , mechanical engineering
The cover picture shows an example of peptide architecture. Variants of the peptide hormone PYY3–36 were designed by addition of a second amphipathic helix to a Lys side chain in the N‐terminal region. The hypothesis was that an increase in membrane binding prior to receptor binding would improve the interaction with the membrane‐bound Y receptors. The background shows the spiral tower of the baroque Church of our Saviour in Copenhagen, Denmark. In contrast to the right‐handed helix, the tower winds in an anticlockwise way. For more details, see the Full Paper by K. J. Jensen, N. Vrang et al. on p. 545 ff.