Figure 2: Experimental partitioning free energy and average membrane orientation of maculatin. | Nature Communications

Figure 2: Experimental partitioning free energy and average membrane orientation of maculatin.

From: Spontaneous formation of structurally diverse membrane channel architectures from a single antimicrobial peptide

Figure 2

(a) CD spectra of the titration of 30 μM maculatin wild type (WT) and mutants with 100 nm POPC LUVs, show that membrane binding is strong ΔGbinding=−4.6±0.8 kcal mol−1. Consistent with the experimental binding the simulations show that at the molecular-level membrane binding is concomitant with interfacial folding of the peptide into a surface-absorbed alpha helix. (b) Oriented CD spectra of WT maculatin in POPC bilayer stacks at 100% relative humidity is 50±15% TM-inserted (peptide-to-lipid ratio=1/30). The dashed lines show theoretical helical spectra for peptides aligned perfectly parallel (red) and perfectly perpendicular (blue) to the beam, corresponding to TM and surface-bound peptides, respectively.

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