Anticancer activity of hydrophobic peptides from soy proteins

Article type: Research Article

Authors: Song E Kim, | Hyuck Hwa Kim, | Ji Yeon Kim, | Young Im Kang, | Hee Jong Woo, | Hyong Joo Lee,

Affiliations: Department of Food Science and Technology | College of Veterinary Medicine, Seoul National University, Suwon, 441-744 Korea

Note: [] Department of Food Science and Technology, College of Agriculture and Life Sciences, Seoul National University, Suwon, 441-744 Korea. Fax: + 82 331 293 4789

Abstract: An anticancer peptide from soy protein was purified and isolated. Defatted soy protein was hydrolyzed with thermoase and hydrophobic peptides were extracted with ethanol. The peptide extract was fractionated by XAD-2 hydrophobic, gel filtration chromatography, and different C18 HPLCs. Anticancer activity of each fraction was assayed by measuring in vitro cytotoxicity on P388D1, a mouse monocyte macrophage cell line. IC_{50} value of a peptide fraction from Sephadex G-25 chromatography was 0.16 mg/ml. This peptide fraction at 1 mg/ml significantly affected cell cycle progression by arresting P388D1 at G2/M phases. Finally purified peptide from analytical C18 HPLC was nonapeptide of which molecular weight was 1157 Da and the sequence was X-Met-Leu-Pro-Ser-Tye-Ser-Pro-Tyr.

Keywords: anticancer, peptide, thermoase hydrolyzates, soy protein

Journal: BioFactors, vol. 12, no. 1-4, pp. 151-155, 2000