Tyrosine is one of the most significant amino acids. They can store the mechanical energy by protein folding and also facilitate proton-mediated electron transport in photosystem II. In our study, we systematically introduced repeating tyrosine units into peptides of various lengths to study the impact of the peptide sequence on self-assembly. The ordering of peptides investigated here has a strong driving force that overcomes the large surface tension of water. We have identified specific sequences of tyrosine containing peptides that can afford densely packed 2D film structure at air/water interface and the resulting structure can withstand the surface tension of water and modify the intrinsic curvature of water droplet. The atomic force microscopy (AFM) analysis along the film edges shows the evidence of film stacking of multiple nano sheets, whose minimum thickness is 1.4 nm. Additionally, the peptide interface presented here provides a tunable platform to template 2D hybrid materials. Consequently, highly ordered 2D assemblies of polypyrrole that cannot be formed by using conventional methods were created for the first time