Abstract
A key therapeutic target in the fight against cancer, the tetramerization domain of the tumor suppressor protein P53 binds a tetraguanidinium ligand at its surface. A specific interaction involving four salt bridges was detected by two NMR-based techniques (see figure). The design of protein-surface ligands is a major challenge because of competition between the ligand and water molecules.
Original language | English (US) |
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Pages (from-to) | 196-198 |
Number of pages | 3 |
Journal | Angewandte Chemie - International Edition |
Volume | 43 |
Issue number | 2 |
DOIs | |
State | Published - Dec 29 2003 |
Keywords
- Host-guest systems
- Ligand design
- Molecular recognition
- NMR spectroscopy
- Proteins
ASJC Scopus subject areas
- Catalysis
- General Chemistry