Antimicrobial peptides (AMPs) as biocides are of great interest because they have the ability to combat antibiotic resistance. Normally, natural AMPs need to be rationally designed or modified for practical use as an antibiotic. Here, a novel AMP, termed FF8, which is a cationic octapeptide composed of arginine, lysine, and phenylalanine, was designed. The FF8 was found to self-assemble into nanofibers when induced by a negatively charged lipid membrane or pH is above 9.4. The fibers on the membrane broke the lipid membrane, forming pores and significantly reducing its fluidity. FF8 also exhibited enhanced antibacterial activity by significantly increasing the permeability of the inner and outer membranes of Escherichia coli (E. coli) and maintaining the pores of the inner membrane of cells, which caused continuous membrane leakage. Because of its high antibacterial activity, cytocompatibility, and cost-effectiveness, FF8 is a promising antibacterial material.

Tyrosinase is a key enzyme involved in melanin synthesis. Therefore, various tyrosinase inhibitors have been screened by researchers in recent years. In the present study, we discovered a novel tyrosinase inhibitor, a peptide ECGYF (named EF-5), with free radical scavenging ability. The effect of tyrosinase inhibition by EF-5 was stronger than that of arbutin and glutathione, when analyzed both in vitro (IC50: 0.46 mM) and in vivo. The UV-Vis absorption and circular dichroism spectroscopies indicated that EF-5 interacted with tyrosinase in a different way as that of glutathione. The results of molecular docking showed that the binding between EF-5 and tyrosinase was determined majorly by hydrogen bonds and hydrophobic interactions. EF-5 had also retained its ability to scavenge both hydroxyl and superoxide radicals in vitro and was found to be nontoxic to cells, as revealed by the MTT assay. These features suggested that the EF-5 peptide may serve as a safe and effective alternative as a tyrosinase inhibitor.

It is believed that the aggregation of amyloid proteins or peptides is promoted by the presence of an air–water interface, and substantial evidence suggests that the characteristics of the air–water interface play critical roles in foam-induced protein aggregation during foam fractionation. However, the effects of the air–water interface on the self-assembly of amyloid-like peptides have not yet been elucidated clearly at the nanometer scale. In this work, air nanobubbles produced in water solution were employed for studying interfacial effects on the self-assembly of a model amyloid peptide termed P11. An atomic force microscopy study showed that the air nanobubbles induced the formation of peptide fibrils with a 9–13 nm helix structure in the P11 solution. Thioflavin T fluorescence and circular dichroism spectroscopic analysis indicated that the nanobubbles induced the change of the peptide conformation to a β-sheet structure. Based on these observations, we have proposed a mechanism to explain how the nanobubbles affect the self-assembly of the P11 peptide at the nanometer scale. Since air nanobubbles are present in water solutions in addition to an air–water interface in normal experiments in vitro, our results indicate that nanobubbles must be taken into account to achieve a complete understanding of protein aggregation events.

In the confinement of a mica–graphene nanocapillary, the self-assembly behaviors of peptides were controlled by the dynamically changing water layers.

Silicone oil induced changes of secondary structures of αB-crystallin (CRYAB) and promoted its aggregation into amyloid-like nanostructures.