Drug discovery and development is a costly and time-consuming process, which requires typically 12–15 years from an original idea to the launch of a final product. The rising importance of protein molecules for the pharmaceutical industry is not only present in the topic of biopharmaceuticals, but also in the case of drug development. Biotherapeutics gain a growing share of the global pharmaceutical market and newly developed products are based on therapeutical proteins such as monoclonal antibodies. Over the last decades, the pharmaceutical market has changed its focus from the production of small molecule components to more complex biopharmaceuticals. Functional characterization studies demonstrate the bioactivity of the proteins and underline the potential for eukaryotic cell-free systems to significantly improve drug development pipelines. In this study, we show the production of druggable target proteins in eukaryotic cell-free systems. Alternative protein production systems, so-called eukaryotic cell-free protein synthesis systems based on eukaryotic cell-lysates, close the gap between a fast protein generation system and a high quality of complex mammalian proteins. Limitations in the production of complex mammalian proteins appear due to inefficient protein folding and posttranslational modifications. Prokaryotic cell-free systems are often the system of choice for drug target protein production due to the simple generation of expression hosts and low cost of preparation. A broad range of protein expression systems is currently available, mostly based on cellular organisms of prokaryotic and eukaryotic origin. The vast majority of drug targets are proteins, which need to be characterized and validated prior to the screening of potential hit components and molecules. In the biopharmaceutical pipeline, protein expression systems are of high importance not only for the production of biotherapeutics but also for the discovery of novel drugs.
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