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Issue 4, 2013
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Structural characterization of a peptoid with lysine-like side chains and biological activity using NMR and computational methods

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Abstract

N-Substituted glycine oligomers or peptoids with charged side chains are a novel class of cell penetrating peptide mimetics and have been shown to serve as drug delivery agents. Here, we investigated by NMR spectroscopy and quantum chemical calculations whether a Rhodamine B labelled peptoid [RhoBSpiro-Ahx]-[But]6ANH2 with lysine-like side chains adopts structural motifs similar to regular peptides. Due to a low chemical shift dispersion, high resolution structure determination with conventional NMR-derived distance restraints and J-couplings was not possible. Instead, a combined assignment and structure refinement strategy using the QM/MM force field COSMOS-NMR was developed to interpret the highly ambiguous chemical shift and distance constraints and obtain a medium resolution three-dimensional structural model. This allowed us to select for the all cis-amide conformation of the peptide with a pseudo-helical arrangement of extended side chains as a faithful representative structure of [RhoBSpiro-Ahx]-[But]6ANH2. We tested the biological activity of the peptoid by live-cell imaging, which showed that the cellular uptake of the peptoid was comparable to conventional cell-penetrating peptides.

Graphical abstract: Structural characterization of a peptoid with lysine-like side chains and biological activity using NMR and computational methods

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Publication details

The article was received on 26 Jul 2012, accepted on 23 Nov 2012 and first published on 26 Nov 2012


Article type: Paper
DOI: 10.1039/C2OB27039K
Citation: Org. Biomol. Chem., 2013,11, 640-647
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    Structural characterization of a peptoid with lysine-like side chains and biological activity using NMR and computational methods

    U. Sternberg, E. Birtalan, I. Jakovkin, B. Luy, U. Schepers, S. Bräse and C. Muhle-Goll, Org. Biomol. Chem., 2013, 11, 640
    DOI: 10.1039/C2OB27039K

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