Structure of micelle bound cationic peptides by NMR spectroscopy using a lanthanide shift reagent

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    Author
    Swarbrick, JD; Karas, JA; Li, J; Velkov, T
    Date
    2020-03-07
    Source Title
    Chemical Communications
    Publisher
    Royal Society of Chemistry
    University of Melbourne Author/s
    Karas, John; Swarbrick, James; Velkov, Tony
    Affiliation
    School of Chemistry
    Pharmacology and Therapeutics
    Biochemistry and Molecular Biology
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    Document Type
    Journal Article
    Citations
    Swarbrick, J. D., Karas, J. A., Li, J. & Velkov, T. (2020). Structure of micelle bound cationic peptides by NMR spectroscopy using a lanthanide shift reagent. Chemical Communications, 56 (19), pp.2897-2900. https://doi.org/10.1039/c9cc09207b.
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    URI
    http://hdl.handle.net/11343/267896
    DOI
    10.1039/c9cc09207b
    Abstract
    [Tm(DPA)3]3- was used to generate multiple, paramagnetic nuclear Overhauser effect NMR spectra of cationic peptides when weakly bound to a lipopolysaccharide micelle. Increased spectral resolution combined with a marked increase in the number of distance restraints yielded high resolution structures of polymyxin and MSI-594 in the liposaccharide bound state.

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