De novo protein surface design: Use of cation-π interactions to enhance binding between an α-helical peptide and a cationic molecule in 50% aqueous solution

Brendan P. Orner, Xavier Salvatella, Jorge Sánchez Quesada, Javier De Mendoza, Ernest Giralt, Andrew D. Hamilton

Research output: Contribution to journalArticle

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 languageEnglish (US)
Pages (from-to)117-119
Number of pages3
JournalAngewandte Chemie - International Edition
Volume41
Issue number1
DOIs
StatePublished - Jan 4 2002

Keywords

  • Helical structures
  • Host-guest systems
  • Molecular recognition
  • NMR spectroscopy
  • Noncovalent interactions

ASJC Scopus subject areas

  • Catalysis
  • Chemistry(all)

Fingerprint Dive into the research topics of 'De novo protein surface design: Use of cation-π interactions to enhance binding between an α-helical peptide and a cationic molecule in 50% aqueous solution'. Together they form a unique fingerprint.

  • Cite this