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Updated: Dec 29, 2025
Fabrication Procedures and Birefringence Measurements for Designing Magnetically Responsive Lanthanide Ion Chelating Phospholipid Assemblies
Published on: January 3, 2018
Structure of micelle bound cationic peptides by NMR spectroscopy using a lanthanide shift reagent
James D Swarbrick1, John A Karas, Jian Li
1Department of Pharmacology and Therapeutics, The University of Melbourne, Parkville, Victoria 3010, Australia. James.swarbrick@unimelb.edu.au james.swarbrick68@gmail.com Tony.velkov@unimelb.edu.au.
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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