Fibroblast growth factors (FGFs) serve numerous regulatory functions in complex organisms, and their corresponding therapeutic potential is of growing interest to academics and industrial researchers alike. However, applications of these proteins are limited due to their low stability. Here we tackle this problem using a generalizable computer-assisted protein engineering strategy to create a unique modified FGF2 with nine mutations displaying unprecedented stability and uncompromised biological function. The data from the characterization of stabilized FGF2 showed a remarkable prediction potential of in silico methods and provided insight into the unfolding mechanism of the protein. The molecule holds a considerable promise for stem cell research and medical or pharmaceutical applications.

Enantis Ltd Biotechnology Incubator INBIT Brno Czech Republic

Faculty of Medicine Department of Biology Masaryk University Brno Czech Republic

Faculty of Science Department of Experimental Biology Loschmidt Laboratories Centre for Toxic Compounds in the Environment RECETOX Masaryk University Brno Czech Republic

Faculty of Science Department of Experimental Biology Masaryk University Brno Czech Republic

International Clinical Research Center St Anne's University Hospital Brno Czech Republic

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CalFitter: a web server for analysis of protein thermal denaturation data