title: Interaction of ATP with fibroblast growth factor 2: biochemical characterization and consequence for growth factor stability.
abstract: BACKGROUND
  Fibroblast growth factor 2, a well-characterized heparin-binding growth factor, is involved in many biological processes like embryogenesis, cell proliferation and angiogenesis. However, this growth factor is very unstable and shows rapid degradation in aqueous solution. Beside the well-known stabilization of FGF2 by heparin or heparan sulphate, the recently discovered binding to ATP also shows a stabilizing and protective effect on this growth factor.
  
  
  RESULTS
  Here we determined the dissociation constant of ATP on FGF2 by equilibrium microdialysis (K(D): 59.8 μM) and analyzed the impact of this binding on secondary structure by CD-spectroscopy. ATP-binding to FGF2 significantly changed the secondary structure of this growth factor with a shift to random coil structure elements. We also analyzed the influence of this binding on the stability of FGF2 in aqueous solution over a period of 2 h. While the amount of untreated FGF2 is reduced drastically over this period of time, ATP-binding reduces the degradation considerably.
  
  
  CONCLUSIONS
  Taken together, our data suggest an important role of ATP in FGF2-stabilization beside the well known-role of heparin and heparan sulphate.
authors: Institut für Pharmazeutische und Medizinische Chemie, Westfälische Wilhelms-Universität Münster, Hittorfstr. 58-62, 48149 Münster, Germany. rosek@uni-muenster.de
authors: Karsten
authors: K
authors: Rose
mesh_terms: D000255:Adenosine Triphosphate / Q000737:chemistry* / Q000378:metabolism; D016222:Fibroblast Growth Factor 2 / Q000737:chemistry* / Q000378:metabolism; D007700:Kinetics; D011485:Protein Binding; D055550:Protein Stability
chemical_list: D016222:Fibroblast Growth Factor 2; D000255:Adenosine Triphosphate