Three peptides containing (RW)n-NH2 units (where n=4, 6, and 8) have been chosen to study the effect of the chain length on the structure and stability of the peptide using Fourier transform infrared (FTIR), scanning electron microscopy (SEM), thermogravimetric analysis (TGA), and differential scanning calorimetry (DSC) techniques. Their interactions with Escherichia coli (E. coli) membrane mimetic vesicles are discussed. Infrared results indicate that addition of (RW)n-NH2 units increases intermolecular H bonds with antiparallel orientation. TGA and DSC results reveal that (RW)6-NH2 shows the optimal chain length in terms of stability and all three peptides show a preferential interaction with one of the anionic lipids in E. coli membranes. SEM images of (RW)4-NH2 present large aggregates while those of (RW)6-NH2 and (RW)8-NH2 present layers of sheet-like structure. In the presence of model membranes, (RW)n-NH2 show fibrillar peptide superstructures. This study suggests that repeating structures of (RW)n-NH2 promotes lateral assembly.
Keywords: (RW)(n) self-assembly; Antimicrobial peptides stability; Antimicrobial peptides structure; Peptide chain length effect.
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