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

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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.

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

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Article information


Submitted
26 Nov 2019
Accepted
17 Jan 2020
First published
24 Jan 2020

Chem. Commun., 2020, Advance Article
Article type
Communication

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

J. D. Swarbrick, J. A. Karas, J. Li and T. Velkov, Chem. Commun., 2020, Advance Article , DOI: 10.1039/C9CC09207B

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