This work describes a novel approach to the realization of ordered protein films. The adopted strategy for the deposition of cytochrome c films involves the synthesis of a compound able to selectively bind arginine residues located at the protein surface. For this purpose, a long alkyl chain alpha-diketone was synthesized; the hydrophobic moiety of this molecule allows the 2-D orientation of modified protein molecules in the film at the air-water interface in a Langmuir-Blodgett trough. NMR and IR spectra confirmed the purity of the synthetized alpha-diketone. X-ray diffraction, ellipsometry, circular dichroism, fluorescence, and W-vis data concerning the diketone and the diketone-modified cytochrome are hereby presented.