Dramatic Enhancement of Binding Affinities Between Foldamer-Based Receptors and Anions by Intra-Receptor π-Stacking

Sung Beom Seo, Seungwon Lee, Hae Geun Jeon, Kyu Sung Jeong

Research output: Contribution to journalArticle

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.

Original languageEnglish
Pages (from-to)10441-10445
Number of pages5
JournalAngewandte Chemie - International Edition
Volume59
Issue number26
DOIs
Publication statusPublished - 2020 Jun 22

All Science Journal Classification (ASJC) codes

  • Catalysis
  • Chemistry(all)

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