Recognition of solvent exposed protein surfaces using anthracene derived receptors

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

Research output: Contribution to journalArticle

Abstract

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
Volume5
Issue number2
DOIs
StatePublished - 2007

Fingerprint

cytochromes
anthracene
Cytochromes c
Membrane Proteins
proteins
Lactalbumin
Pancreatic Ribonuclease
Myoglobin
Reducing Agents
Muramidase
Coulomb interactions
Static Electricity
Heme
Scaffolds
Quenching
myoglobin
Fluorescence
Phosphates
lysozyme
affinity

ASJC Scopus subject areas

  • Biochemistry, Genetics and Molecular Biology(all)
  • Chemistry(all)

Cite this

Recognition of solvent exposed protein surfaces using anthracene derived receptors. / Wilson, Andrew J.; Hong, Jason; Fletcher, Steven; Hamilton, Andrew.

In: Organic and Biomolecular Chemistry, Vol. 5, No. 2, 2007, p. 276-285.

Research output: Contribution to journalArticle

Wilson, Andrew J. ; Hong, Jason ; Fletcher, Steven ; Hamilton, Andrew. / Recognition of solvent exposed protein surfaces using anthracene derived receptors. In: Organic and Biomolecular Chemistry. 2007 ; Vol. 5, No. 2. pp. 276-285.
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