A Tetraguanidinium Ligand Binds to the Surface of the Tetramerization Domain of Protein P53

Xavier Salvatella, Marc Martinell, Margarida Gairí, Mauricio G. Mateu, Miguel Feliz, Andrew D. Hamilton, Javier De Mendoza, Ernest Giralt

Research output: Contribution to journalArticlepeer-review

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 languageEnglish (US)
Pages (from-to)196-198
Number of pages3
JournalAngewandte Chemie - International Edition
Volume43
Issue number2
DOIs
StatePublished - Dec 29 2003

Keywords

  • Host-guest systems
  • Ligand design
  • Molecular recognition
  • NMR spectroscopy
  • Proteins

ASJC Scopus subject areas

  • Catalysis
  • Chemistry(all)

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