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Inside Cover: Prolinoamino Acids as Tools to Build Bifunctionalized, Stable β‐Turns in Water (ChemBioChem 1/2010)
Author(s) -
Mothes Céline,
Larregola Maud,
Quancard Jean,
Goasdoué Nicole,
Lavielle Solange,
Chassaing Gérard,
Lequin Olivier,
Karoyan Philippe
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.200990091
Subject(s) - peptidomimetic , cover (algebra) , amino acid , chemistry , nuclear magnetic resonance spectroscopy , turn (biochemistry) , stereochemistry , side chain , combinatorial chemistry , organic chemistry , peptide , biochemistry , engineering , polymer , mechanical engineering
The inside cover picture shows a pseudotetrapeptide incorporating a cis ‐3‐prolinoamino acid and an N ‐methylamino acid. This peptidomimetic adopts a stable β‐turn conformation in water, as shown by CD and NMR spectroscopy. 3‐Substituted prolines are valuable tools for synthesizing β‐turn mimetics while keeping the side chain of proteinogenic amino acids. For further details, see the communication by O. Lequin, P. Karoyan et al. on p. 55 ff.