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Dramatic Enhancement of Binding Affinities Between Foldamer‐Based Receptors and Anions by Intra‐Receptor π‐Stacking
Author(s) -
Seo Sung Beom,
Lee Seungwon,
Jeon HaeGeun,
Jeong KyuSung
Publication year - 2020
Publication title -
angewandte chemie
Language(s) - English
Resource type - Journals
eISSN - 1521-3757
pISSN - 0044-8249
DOI - 10.1002/ange.202002657
Subject(s) - affinities , foldamer , chemistry , stacking , folding (dsp implementation) , receptor , hydrogen bond , stereochemistry , crystallography , binding affinities , binding pocket , ligand (biochemistry) , binding site , molecule , biophysics , combinatorial chemistry , biochemistry , organic chemistry , biology , electrical engineering , engineering
Abstract As a synthetic model for intra‐protein interactions that reinforce binding affinities between proteins and ligands, the energetic interplay of binding and folding was investigated using foldamer‐based receptors capable of adopting helical structures. The receptors were designed to have identical hydrogen‐bonding sites for anion binding but different aryl appendages that simply provide additional π‐stacking within the helical backbones without direct interactions with the bound anions. In particular, the presence of electron‐deficient aryl appendages led to dramatic enhancements in the association constant between the receptor and chloride or nitrate ions, by up to three orders of magnitude. Extended stacking within the receptor contributes to the stabilization of the entire folding structure of complexes, thereby enhancing binding affinities.