Complex Effects of Molecular Chaperones on the Aggregation and Refolding of Fibroblast Growth Factor-1

摘要: Abstract Fibroblast growth factor one (FGF-1) exists in a molten globule (MG)-like state under physiological conditions (neutral pH, 37°C). It has been proposed that this form of the protein may be involved its atypical membrane transport properties. Macromolecular chaperones have shown to bind MG states proteins as well transport. We therefore examined effect such on aggregation and refolding FGF-1 evaluate whether they might play role The chaperone α-crystallin was found strongly inhibit FGF-1. Curiously, two other similar size charge (thyroglobulin monoclonal IgM immunoglobulin) with no previously reported properties were also related effect. In contrast, GroEL/ES induced further MG-like but had native conformation. Both stimulated (25°C) detectable when refolded (37°C). This suggests disordered intermediates are present folding pathways FGF conformations which differ from conditions. does, therefore, interact molecular chaperones, although involve both protein.