Acetylcholine Recognition by a Deep, Biomimetic Pocket

Authors

  • Fraser Hof,

    1. The Department of Chemistry and, the Skaggs Institute for Chemical Biology, The Scripps Research Institute, 10550 N. Torrey Pines Rd., MB-26, La Jolla, CA, 92037, USA, Fax: (+1) 858-784-2876
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    • These authors contributed equally to this work.

  • Laurent Trembleau,

    1. The Department of Chemistry and, the Skaggs Institute for Chemical Biology, The Scripps Research Institute, 10550 N. Torrey Pines Rd., MB-26, La Jolla, CA, 92037, USA, Fax: (+1) 858-784-2876
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    • These authors contributed equally to this work.

  • Elke Christine Ullrich,

    1. The Department of Chemistry and, the Skaggs Institute for Chemical Biology, The Scripps Research Institute, 10550 N. Torrey Pines Rd., MB-26, La Jolla, CA, 92037, USA, Fax: (+1) 858-784-2876
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  • Julius Rebek, Jr. Prof.

    1. The Department of Chemistry and, the Skaggs Institute for Chemical Biology, The Scripps Research Institute, 10550 N. Torrey Pines Rd., MB-26, La Jolla, CA, 92037, USA, Fax: (+1) 858-784-2876
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  • This research was supported by the Skaggs Institute for Chemical Biology and the NIH (GM 27932). E.C.U. thanks the Deutsche Forschungsgemeinschaft for fellowship support. The authors thank Prof. Pablo Ballester for helpful discussions.

Abstract

original image

Four negative charges at the entrance of a deep pocket, lined with aromatic residues are the features of a synthetic receptor which shows high affinity for acetylcholine (see picture) and choline in water. The size, shape, and charge recognition elements featured in the natural enzyme acetylcholinesterase are reproduced by the synthetic receptor.

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