The market for monoclonal antibodies is continuously growing due to their high specificity and applicability in diagnostics and therapy. Also, small engineered scaffold proteins are getting more attention as an alternative to the market-leading antibodies, thanks to their high stability, low immunogenicity and low production cost. However, their small size might lead to fast blood clearance, which can be an advantage for imaging purposes but can become a disadvantage in a therapeutic setting. To overcome this, a new protein library based on Albumin-derived affinity proteins (ADAPTs) was designed, originating from a bacterial albumin-binding domain. From this library, it was possible to achieve protein modules with ability to bind to its intended target as well as to -albumin, a feature that is believed to increase the binder’s half-life in the body. Binding modules could be achieved by performing phage display selections towards Tumor necrosis factor alpha (TNFa) and Interleukin-17c (IL17c), both important proinflammatory cytokines and possibly interesting targets for therapeutical applications. The selection output was analyzed using Next Generation Sequencing (NGS) and promising candidates were cloned and produced in Escherichia coli. Followed by detailed characterization it was possible to generate binders with high affinity and stability showing bispecific binding to its respective targets or albumin. Each binder was then examined for their usefulness as a real therapeutic by successfully evaluating its ability to block the interaction of the cytokine and its specific receptor in vitro. This newly developed protein binders, showing high affinity towards their targets as well keeping its initial binding to albumin present another possibility to combine the advantages of small engineered scaffold proteins with those of typical larger proteins allowing for more convenient production in bacteria leading to lower production costs and making them therefore ideal candidates for future therapeutics.