Nevertheless, the utilization of biomolecules, i.e., proteins, to impart functionality to inorganic and/or organic materials and afford highly efficient functional devices presents a number of challenges in the research of functional biomaterials. [4][5][6] The main limitations predominantly arise from intermolecular aggregation, surfaceinduced denaturation, steric hindrance of active sites, and lack of dynamical freedom imposed by solid state. [7][8][9] The deposition of continuous protein thin films seems to be a good strategy that fulfill those needs. [10,11] With particular emphasis on biocatalytic coatings, the fabrication method should guarantee high enzyme loads, low substrate/product flow transport limitations, and improve the lifetime and stability of the biomolecule. [12] Currently, reported methods for the fabrication of functional biofilms are based on the utilization of a relatively limited range of naturally self-assembling proteins, layer-by-layer deposition approaches, and the adsorption of the proteins to amphiphilic copolymers. [13][14][15][16][17] However, these approaches usually require of the covalent crosslinking of the components in order to avoid the disaggregation of the film in water and at broad range of pH. [18] Yet, the uncontrolled covalent crosslinking might be especially damaging in the formation of functional protein films. The protein's amino acids can be altered and severe substrate diffusion issues might be caused within the film, resulting in impaired biomaterials. [19] Therefore, an alternative sequence-independent methodology that allows the fabrication of functional protein films would vastly expand the toolkit for creating biomaterials.In this regard, the bioinspired self-assembly of hierarchically structured peptide or protein films is an attractive approach. [20][21][22][23] In nature, the metal-driven crosslinking of specific peptidic building blocks leads to complex hierarchical structures across many lengths, as it happens in mussel byssus or worm jaws. [24][25][26] Furthermore, metal-directed protein selfassembly (MDPSA) methodology is inspired by the affinity of distinct residue side chains such as histidines, cysteines, lysines, and asparagines toward metallic cations (mainly Ni, Cu, Co, and Zn). MDPSA allocates such key residues on the surface of the protein as anchoring points. [27][28][29] Hence, metal ions are used as inorganic bridges that not only guide the assembly of the proteins into hierarchical architectures, but also might The deposition of protein thin films on (in)organic surfaces is a key approach to incorporate new functionalities into these materials for a broad number of applications. However, most of the current methods used for the controlled assembly of such biomolecules and eventual film formation are limiting since entail either the chemical modification of the proteins, which leads sometimes to impaired materials, or the sequential layer-by-layer deposition of charged macromolecules. In this work, a facile bioinspired method for the versati...