Figure 3: Spontaneous membrane insertion and intra-membrane oligomerization of maculatin. | Nature Communications

Figure 3: Spontaneous membrane insertion and intra-membrane oligomerization of maculatin.

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

Figure 3

(a) All peptides initially reside in the surface-bound state in the upper membrane leaflet (ribbons coloured blue to red from N to C terminus, charged and polar side chains shown). (b) Over the course of 50 μs, the peptides first insert TM, translocate to the other bilayer leaflet and then form various oligomers, resulting in an equal distribution of the peptide mass across the membrane. This process is completed after ∼15 μs. The centre of mass positions of two representative peptides are shown in red and black. (c) Tilt angles of all peptides, showing their numerous transitions between surface-bound and TM-inserted states. (d) Dimers, trimers and tetramers both form and dissolve rapidly on a microsecond scale. Monomeric surface-bound states dominate (S, blue), but oligomers, both parallel and antiparallel, occur 29% of the simulation time for this simulation, in all other simulations the oligomer population is 47% (see below). The TM monomer is show in light yellow and higher colour oligomers are shown in darker tones of yellow to orange. A representative antiparallel tetramer is shown at 32 μs.

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