Answers are grounded in this paper and cite their sources.
Presentation 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.
No takes yet. Share an insight, caveat, or question.
Lühmann et al. (2015) studied this question.
Synapse has enriched 10 related papers. Consider them for comparative context: