Recognition of solvent exposed protein surfaces using anthracene derived receptors

Andrew J. Wilson, Jason Hong, Steven Fletcher, Andrew D. Hamilton

Research output: Contribution to journalArticlepeer-review


A new class of receptor is described that can selectively bind to the solvent exposed surface of proteins such as cytochrome c and lysozyme with low micromolar affinity over cytochrome c551, α-lactalbumin, myoglobin and RNase A, under physiologically relevant conditions (5 mM phosphate, pH 7.4). The use of anthracene as a hydrophobic scaffold allows the receptor to act as a selective chemosensor via fluorescence quenching or FRET. The study reveals that co-operative electrostatic interactions over a large surface area dominate binding. Further investigations reveal that the receptor binds to the solvent exposed heme edge of cytochrome c inhibiting its reaction with small reducing agents and validating the strategy for the disruption of protein function.

Original languageEnglish (US)
Pages (from-to)276-285
Number of pages10
JournalOrganic and Biomolecular Chemistry
Issue number2
StatePublished - 2007

ASJC Scopus subject areas

  • Biochemistry
  • Physical and Theoretical Chemistry
  • Organic Chemistry


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