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Issue 2, 2007
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Recognition of solvent exposed protein surfaces using anthracene derived receptors

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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.

Graphical abstract: Recognition of solvent exposed protein surfaces using anthracene derived receptors

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Publication details

The article was received on 11 Sep 2006, accepted on 02 Nov 2006 and first published on 05 Dec 2006


Article type: Paper
DOI: 10.1039/B612975G
Citation: Org. Biomol. Chem., 2007,5, 276-285

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    Recognition of solvent exposed protein surfaces using anthracene derived receptors

    A. J. Wilson, J. Hong, S. Fletcher and A. D. Hamilton, Org. Biomol. Chem., 2007, 5, 276
    DOI: 10.1039/B612975G

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