Synthesis of a Peptide Emulsifier with an Amphiphilic Structure

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Three kinds of peptides (H, S, and R) with 16 amino acid residues were synthesized, and their secondary structure and emulsifying properties (emulsifying activity and oil-binding property) were investigated to clarify the effects of conformational amphiphilicity. The amino acid compositions of the three peptides were the same (8 Leu and 8 Glu residues) but their sequences were different. Circular dichroism analysis showed that peptide H contained an α-helix at pH 5. 5 but took a random structure at pH 7. 0. Peptide S also cotnained an α-helix at pH 5. 5, while a β-sheet structure was predominant at pH 7. 0. Peptide R took mainly a random structure at both pH 5. 5 and pH 7. 0. The helical properties of peptide H and peptide S were different ; the α-helix of peptide H was amphiphilic, while that of peptide S was not. Under conditions where peptide H formed an amphiphilic α-helix, both the emulsifying activity and oil-binding property of the peptide signiticantly increased. The emulsifying properties of peptide S, which formed an amphiphilic β-sheet at pH 7. 0, were also good at that pH. We conclude that a peptide with an amphiphilic α-helix or β-sheet structure has better emulsifying properties, hence a good peptide emulsifier could be designed by incorporating such a structure.
社団法人日本農芸化学会の論文
1995-03-23