Antioxidant activity of designed peptides based on the antioxidative peptide isolated from digests of a soybean protein

Antioxidative activities of 28 synthetic peptides, which were designed based on an antioxidative peptide (Leu-Leu-Pro-His-His) derived from proteolytic digests of a soybean protein, against the peroxidation of linoleic acid in an aqueous system were measured by the ferric thiocyanate method. The results for the hydroperoxide levels derived from linoleic acid agreed with those obtained by reversed-phase high-performance liquid chromatography. The deletion of the C-terminal His decreased the activity, whereas the deletion of the N-terminal Leu had no effect. In the peptide sequence, His and Pro played important roles in the antioxidative activity and, among the peptides tested, Pro-His-His was the most antioxidative. The activity decreased on substitution of the second His with D-His. Introduction of Tyr to the positions of Pro or His did not increase the activities of the corresponding peptides. Antioxidative peptides showed synergistic effects with nonpeptidic antioxidants as observed in soybean protein hydrolysates. The magnitude of the effects, however, did not correlate with the antioxidative activities of the peptides.