Abstract
The relative position of the Asp and Trp residues in a peptide chain is important for recognizing a tetraguanidinium receptor through hydrogen bonding and cation-π interactions. The molecule not only binds with high affinity (Ka = 1.1 x 108M-1), it also stabilizes the helical schematic representation) as demonstrated by NMR and CD spectroscopy.
Original language | English (US) |
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Pages (from-to) | 117-119 |
Number of pages | 3 |
Journal | Angewandte Chemie - International Edition |
Volume | 41 |
Issue number | 1 |
DOIs | |
State | Published - Jan 4 2002 |
Keywords
- Helical structures
- Host-guest systems
- Molecular recognition
- NMR spectroscopy
- Noncovalent interactions
ASJC Scopus subject areas
- Catalysis
- Chemistry(all)