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.