Fibrous proteins such as silk fibroin, keratin and elastin are able to mimic the extracellular matrix that allows their recognition under physiological conditions. The impressive mechanical properties, environmental stability, in combination with their biocompatibility and control of morphology, provide an important basis to use these proteins in biomedical applications. This work exploits the self-assemble properties of these proteins for the development of new materials to be used as wound dressings: evaluation of the blending effect on the physical and chemical properties of the materials; development of materials with different morphologies; assessment of the cytocompatibility of the protein matrices; use of innovative short peptide sequences that allow to target the control of high levels of HNE found on chronic wounds. The motivation for this work was to combine the excellent properties of silk fibroin with other proteins. Silk fibroin is widely characterized in the literature for the production of biomaterials, but this work is the first that successfully evaluates the blends silk fibroin/keratin and silk fibroin/elastin for their application as wound dressings.