Table 3. Sequences and CD Structural Characteristics of Peptide Variants R69D/K74D, K74D, K74L, N77K, and F72S Derived from the Identified Membrane-Binding Motif (AB2N)a.
| name | sequence | net charge | μH | H face | Δ[θ]MRE,222nm | AH |
|---|---|---|---|---|---|---|
| AB2N | YSRLGFGKALNSLWLHGLLP | +2.25 | 0.129 | Y | –17.3 ± 1.2 | Y |
| R69D/K74D | YSDLGFGDALNSLWLHGLLP | –1.75 | 0.133 | Y | –0.1 ± 1.0 | N |
| K74D | YSRLGFGDALNSLWLHGLLP | +0.25 | 0.119 | Y | –0.7 ± 0.5 | N |
| K74L | YSRLGFGLALNSLWLHGLLP | +1.25 | 0.090 | Y | ND | N |
| N77K | YSRLGFGKALKSLWLHGLLP | +3.35 | 0.128 | Y | –7.6 ± 0.6 | Y |
| F72S | YSRLGSGKALNSLWLHGLLP | +2.25 | 0.112 | N | –0.8 ± 0.5 | N |
a
The amino acids that were the targets for variations are highlighted by style. The positively charged residues R and K are bold, the negatively charged residue D is bold-italic, the polar residue S is underlined, and the hydrophobic residues F and L are italic. μH: hydrophobic moment calculated by HeliQuest, AH: amphipathic Helix, ND: not determined.