Extended Data Fig. 2: Hydrophobic residues of the β-loop and the N-loop anchor plectasin in the membrane. | Nature Microbiology

Extended Data Fig. 2: Hydrophobic residues of the β-loop and the N-loop anchor plectasin in the membrane.

From: Host defence peptide plectasin targets bacterial cell wall precursor lipid II by a calcium-sensitive supramolecular mechanism

Extended Data Fig. 2

A,B) T2-edited 1H(1H)13C experiments5 of 13C15N-plectasin in complex with Lipid II probing membrane insertion. In this experiment, after a T2-filter that destroys magnetization on rigid moieties, magnetization from mobile water and lipid molecules is transferred to the rigid antibiotic using 1H1H mixing, and eventually read out on 13C using a short cross-polarization. A) Top: 1D spectrum displaying mobile lipid resonances after dephasing of rigid plectasin resonances using a T2-filter of 2.5 ms and no 1H1H mixing. Middle: T2-edited 2D 1H(1H)13C experiment with a T2-filter of 2.5 ms and 1H1H mixing time of 5 ms. Bottom: 1D 13C CP spectrum of the complex. B) ssNMR-derived membrane topology mapped onto plectasin. Residues that help to anchor plectasin in the membrane are highlighted in brown colors, the water-exposed Ile22 is colored in blue. C) ssNMR contact between I22 and Y25. Overlay of two 2D 13C13C PARIS-xy4 spectra of 13C15N-plectasin in complex with lipid II in membranes with either a short (62 ms, green) or long (600 ms, blue) mixing time. Spectra were recorded at a magnetic field of 950 MHz (1H-frequency), a sample temperature of 270 K and 18 kHz MAS.

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