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

Chem Commun (Camb). 2020 Mar 7;56(19):2897-2900. doi: 10.1039/c9cc09207b. Epub 2020 Feb 10.

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.

MeSH terms

  • Antimicrobial Cationic Peptides / chemistry*
  • Indicators and Reagents / chemistry
  • Lanthanoid Series Elements / chemistry*
  • Micelles*
  • Nuclear Magnetic Resonance, Biomolecular / methods*
  • Peptides / chemistry
  • Polymyxin B / chemistry
  • Protein Conformation

Substances

  • Antimicrobial Cationic Peptides
  • Indicators and Reagents
  • Lanthanoid Series Elements
  • MSI 594
  • Micelles
  • Peptides
  • Polymyxin B