This article has been reviewed according to Science X's editorial process and policies. Editors have highlighted the following attributes while ensuring the content's credibility: A new study published in the Biophysical Journal reports on the development of a stable, biologically active version of the human fibroblast growth factor. Human fibroblast growth factor, or FGF, has potent wound-healing and antidiabetic properties that could prove useful in the development of new therapeutics.
The novel mechanism by which the researchers were able to enhance the structural stability and cell proliferative activity of FGF has been patent-protected. "FGFs are very important molecules," said Suresh Kumar Thallapuranam, corresponding author on the study and a University Professor of chemistry and biochemistry at the U of A. "In fact, I would say that they are the essence of life.
Without FGF, there is no life. From the day we are born as a single cell in our mother's womb, the cells multiply. And for that multiplication, FGF is required." He added that FGF is not just crucial to the proliferation of cells, but also to their differentiation into other cells.
But it's FGF's former role in the proliferation of cells that has researchers eyeing its therapeutic value, potentially playing a role in enhancing the tissue repair process, which is greatly slowed in metabolic diseases like chronic diabetes, leading to infections and even amputations. The study was more than 10 years in the making, during which Thallapuranam and his collaborators teased out the three-dimensional structure of human FGF and then unraveled the mechanism by which it binds to heparin and facilitates the signaling of proteins that regulate essential biological processes. In its natural form in the body, human FGF is unstable and has a short biological half-life, likely as an evolutionary hedge against the kind of unchecked cell proliferation that can result in cancer.
The science is complex, but with the help of advanced, multidimensional nuclear magnetic resonance spectroscopy, Thallapuranam and his colleagues were able to manipulate the charges that typically bind FGF to heparin proteins (biomedically, heparin is often used as an anticoagulant). The researchers developed and inserted a charge-reversal mutation, named R126E, into the "heparin binding pocket" that markedly enhanced the structural stability and proliferative activity of FGF. It was the development of this charge-reversal mutation that earned the work patent protection.
It also laid the foundation for development of what Thallapuranam calls a "super FGF." While this is beyond the scope of the current paper, Thallapuranam says that super FGF has important metabolic properties, helping cells oxidize fatty acids and glucose and clear cholesterol, which would be beneficial in the treatment of obesity. Julie Eberle Davis et al, Charge reversal in the heparin-binding pocket enhances the stability and activity of the human FGF1, Biophysical Journal (2026). DOI: 10.1016/j.bpj.2026.06.037 Journal information: Biophysical Journal BSc Life Sciences & Ecology.
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