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Cover Feature: Increased Conformational Flexibility of a Macrocycle–Receptor Complex Contributes to Reduced Dissociation Rates (Chem. Eur. J. 64/2017)
Author(s) -
Glas Adrian,
Wamhoff EikeChristian,
Krüger Dennis M.,
Rademacher Christoph,
Grossmann Tom N.
Publication year - 2017
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.201704109
Subject(s) - isothermal titration calorimetry , cover (algebra) , chemistry , flexibility (engineering) , dissociation (chemistry) , kinetics , nuclear magnetic resonance spectroscopy , peptidomimetic , stereochemistry , biophysics , crystallography , peptide , biochemistry , physics , mathematics , biology , mechanical engineering , statistics , engineering , quantum mechanics
State‐of‐the‐art isothermal titration calorimetry, 19 F NMR spectroscopy and molecular dynamics simulations reveal unexpected differences in the binding kinetics of closely related macrocycles. Most strikingly, increased flexibility of the bound macrocycle correlates with elongated receptor residence time. These findings highlight the potential of loop‐like peptide epitopes as starting point for macrocyclic peptidomimetics. More information can be found in the Communication by C. Rademacher, T. N. Grossmann et al. on page 16157.