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Magnetic resonance imaging

Making sense of disassembly

Nature Chemistry volume 1, pages 523–524 (2009)Cite this article

An amphiphilic molecule that contains a protein-specific ligand and an NMR-active tag forms the basis of a protein sensor. A measurable NMR signal results only in the presence of active protein that causes disassembly of clusters of the amphiphile.

Most human diseases are primarily based on protein imbalances, which makes the ability to sense proteins in complex environments important. Sensing a target analyte necessarily involves two steps: first, recognizing the presence of the analyte, such as through ligand–receptor binding, and second, transducing this binding event into a readable signal. Nature demonstrates unmatched expertise in both areas, and can use a specific protein-binding event to trigger a cascade of biological processes. Although chemists have made reasonable strides in designing ligands that complement the active sites of specific proteins in a complex mixture, designing pathways to signal that recognition event has been a daunting challenge. Writing on page 557 of this issue, Itaru Hamachi and colleagues from Kyoto University report on a new approach in which well-defined spectroscopic signatures are generated to signal a specific ligand–receptor binding event1.

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Figure 1: Protein-induced disassembly of aggregates generates an NMR or MRI signal.

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Affiliations

  1. Malar A. Azagarsamy and S. Thayumanavan are in the Department of Chemistry, University of Massachusetts, Amherst, Massachusetts 01003, USA.

    Malar A. Azagarsamy & S. Thayumanavan

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  1. Malar A. Azagarsamy
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  2. S. Thayumanavan
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Correspondence to S. Thayumanavan.

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Azagarsamy, M., Thayumanavan, S. Making sense of disassembly. Nature Chem 1, 523–524 (2009). https://doi.org/10.1038/nchem.383

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