Under certain conditions, hydrolysis of the peptide bond catalyzed by protease can be reversed for peptide bond formation. A few protease have been successfully applied to the preparation of small peptides of pharmaceutical and nutritional interests in organic solvents. However, becasue of the low solubility of hydrophilic amino acid substrates in organic media, the hydrophilic peptide synthesis became more difficult than that of hydrophobic peptides. In organic solvents, the synthesis of hydrophilic amino acid-containing peptides always has a rather low yield. The main aim of this study is to solve the problem with low solubility of hydrophilic amino acid substrates in orgaic solvents. RGD, the tripeptide Arg-Gly-Asp is a kind of cellular binding factor which ahs the ability of cell adhesion. It is valuable as a new drug for curing burn injury In addition, RGD tripeptide contains two hydrophilic amino acids(Arg and Asp)>
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