抄録
In the present study, we identified and chemically synthesized two cationic peptides, Amyl-1-18 and BCBS-11, which are derived from rice and soybean proteins, respectively. These peptides had high isoelectric points, high positive net charges, and included multiple hydrophobic amino acids. Subsequently, we identified multiple functions of the two peptides, including antimicrobial, lipopolysaccharide-neutralizing, and angiogenic activities. We also examined their cytotoxic activities against mammalian red blood cells. Amyl-1-18 and BCBS-11 exhibited antimicrobial activity against Porphyromonas gingivalis, Streptococcus mutans, and Candida albicans. Membrane-depolarization assays and flow cytometric analyses showed that the antimicrobial properties of Amyl-1-18 and BCBS-11 against P. gingivalis and S. mutans were dependent on membrane-disrupting potential. In contrast, major antimicrobial activities of the two peptides against C. albicans were dependent on interactions with targets other than cell membranes. Furthermore, chromogenic Limulus amebocyte lysate assays showed that the two peptides (50% effective concentrations, EC50; 0.22-0.31 µM) neutralize LPS with similar potency (EC50: 0.11 µM) to that of polymyxin B. Moreover, tube-formation assays in human umbilical vein endothelial cells showed similar angiogenic activities of the two peptides as those following treatment with LL-37. The rate of hemolysis for Amyl-1-18 and BCBS-11 in the presence of 250-µM was less than 2%. These results demonstrate that cationic peptides from food proteins have potential as multifunctional ingredients for healthcare applications.
