Gutmann, MarcusMarcusGutmannRybak, Jens-ChristophJens-ChristophRybakNickel, JoachimJoachimNickelRubini, MarinaMarinaRubiniMeinel, LorenzLorenzMeinelLühmann, TessaTessaLühmannJones, GabrielGabrielJones2022-03-052022-03-052015https://publica.fraunhofer.de/handle/publica/24178910.1021/acsbiomaterials.5b00236Presentation of therapeutic proteins on material surfaces is challenged by random immobilization chemistries through lysine or cysteine residues, typically leading to heterogeneous product outcome. Pharmaceutical quality standards warrant a controlled process ideally through site specific conjugation. Therefore, we deployed genetic codon expansion to engineer a propargyl-l-lysine (Plk)-modified FGF-2 analogue, enabling site-specific copper(I)-catalyzed azide alkyne cycloaddition (CuAAC). Site-specific decoration of Plk-FGF-2 to particles sparked cell proliferation of human osteosarcoma cells in a spatially controlled manner around the decorated carrier, rendering this approach instrumental for the future design of quality-improved bioinstructive scaffold outcome.enfibroblast growth factor 2 (FGF-2)bio-orthogonal immobilizationgenetic codon expansiondecorationproliferationjournal article