Stable engineered human fibroblast growth factor created for therapeutic research

A team of researchers has announced a breakthrough in protein engineering, reporting in the *Biophysical Journal* the creation of a stable, biologically active form of human fibroblast growth factor (FGF). The study details how the modified protein retains the key functional domains required for cell signaling while exhibiting markedly improved thermal stability and resistance to proteolytic degradation—issues that have historically limited the therapeutic use of FGF.

The enhanced FGF variant was engineered through targeted amino‑acid substitutions that preserve its receptor‑binding interface yet reduce conformational flexibility. In vitro assays demonstrated that the protein maintains its ability to stimulate fibroblast proliferation and to promote wound‑healing pathways, while also exhibiting antidiabetic activity by enhancing insulin sensitivity in cultured adipocytes. The authors suggest that this stabilized form could serve as a more reliable candidate for drug development, potentially enabling oral or topical formulations that were previously unfeasible.

If these findings translate to in vivo models, the new FGF construct could accelerate the development of treatments for chronic wounds and metabolic disorders. The research team plans to advance preclinical studies to evaluate safety, dosing, and delivery strategies, with the ultimate goal of moving toward clinical trials.