Journal article
Structure of micelle bound cationic peptides by NMR spectroscopy using a lanthanide shift reagent
James D Swarbrick, John A Karas, Jian Li, Tony Velkov
Chemical Communications | Royal Society of Chemistry | Published : 2020
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.
Grants
Funding Acknowledgements
J. L. and T. V. are supported by grants from the Australian National Health and Medical Research Council as Senior Research and Career Development Fellows. We thank Bio21 for access to the NMR facility.