Figure 1 | Scientific Reports

Figure 1

From: Effect of hydrophobic moment on membrane interaction and cell penetration of apolipoprotein E-derived arginine-rich amphipathic α-helical peptides

Figure 1

Structural isomers of amphipathic α-helical A2-17. The helical wheel diagrams for amino acid sequences of A2-17 R10L/L11R, A2-17 R7L/L8R, A2-17, and A2-17 L14R/R15L arranged as an ideal α-helix (100° rotation per residue) seen down the long axis from the amino-terminal end. The hydrophobic moment (μH), as a measure of amphipathicity of α-helix, for each peptide was calculated using the MPEx software (https://blanco.biomol.uci.edu/mpex/). The bold arrows represent hydrophobic moments as vectors. The hydrophobic domain of the helical wheel is shown by a semi-circle, at which a dotted arrow represents the position vector of Trp residue. The value α is the angle between the hydrophobic moment and the position vector of the Trp residue in the helical wheel diagram.

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