A pH-responsive polymer Eudragit S-100 has been found to assist in correct folding of FGF-2 （fibroblast growth factor-2） denatured with 8 mol/L urea and 10 mmol/L dithiothreitol at pH 7.2. The refolding of FGF-2 was...A pH-responsive polymer Eudragit S-100 has been found to assist in correct folding of FGF-2 （fibroblast growth factor-2） denatured with 8 mol/L urea and 10 mmol/L dithiothreitol at pH 7.2. The refolding of FGF-2 was performed by directly diluting denatured FGF-2 into a refolding buffer containing Eudragit S-100. The ability of Eudragit S-100 to enhance protein refolding level was investigated using MTT method, fluorescence emission spectroscopy and reverse phase HPLC. On the other hand, the result shows the ability of Eudragit S-100 to enhance the refolding level of protein is due to the interaction between Eudragit S-100 and oositivelv charaed FGF-2.展开更多
A new product PEGylated rhaFGF was obtained by site-directed chemical modification.When compared with unmodified rhaFGF, PEGylated rhaFGF showed comparable bioactivity and superior stability at 37℃ in mouse serum and...A new product PEGylated rhaFGF was obtained by site-directed chemical modification.When compared with unmodified rhaFGF, PEGylated rhaFGF showed comparable bioactivity and superior stability at 37℃ in mouse serum and the stronger resistant potency to trypsin. This was accompanied by a substantial decreasing tmmunogenicity.Site-specific PEGylation of rhaFGF may increase its therapeutic potency in humans.展开更多
基金supported by grants from the Hi-tech Research and Development Program of China(No.2007AA02Z110)Key Grant of Wenzhou Department of Science and Technology(No.Y2007A106)+1 种基金Grant of Guangzhou Department of Science and Technology(No.GK0701013)Grant from Health Bureau of Zhejiang (No.B135).
文摘A pH-responsive polymer Eudragit S-100 has been found to assist in correct folding of FGF-2 （fibroblast growth factor-2） denatured with 8 mol/L urea and 10 mmol/L dithiothreitol at pH 7.2. The refolding of FGF-2 was performed by directly diluting denatured FGF-2 into a refolding buffer containing Eudragit S-100. The ability of Eudragit S-100 to enhance protein refolding level was investigated using MTT method, fluorescence emission spectroscopy and reverse phase HPLC. On the other hand, the result shows the ability of Eudragit S-100 to enhance the refolding level of protein is due to the interaction between Eudragit S-100 and oositivelv charaed FGF-2.
基金The Hi-tech Research and Development Program of China(2002AA2Z3318)Guangdong Natural Science Foundation(010424)supported this study.
文摘A new product PEGylated rhaFGF was obtained by site-directed chemical modification.When compared with unmodified rhaFGF, PEGylated rhaFGF showed comparable bioactivity and superior stability at 37℃ in mouse serum and the stronger resistant potency to trypsin. This was accompanied by a substantial decreasing tmmunogenicity.Site-specific PEGylation of rhaFGF may increase its therapeutic potency in humans.
