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

James D. Swarbrick, John A. Karas, Jian Li, Tony Velkov

Research output: Contribution to journalArticleResearchpeer-review

1 Citation (Scopus)


[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.

Original languageEnglish
Pages (from-to)2897-2900
Number of pages4
JournalChemical Communications
Issue number19
Publication statusPublished - 7 Mar 2020

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