Anticancer activity of hydrophobic peptides from soy proteins

Song E. Kim; Hyuck Hwa Kim; Ji Yeon Kim; Young Im Kang; Hee Jong Woo; Hyong Joo Lee

doi:10.1002/biof.5520120124

Anticancer activity of hydrophobic peptides from soy proteins

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

Dept. of Food Science and Technology

Seoul National University

Research output: Contribution to journal › Article › peer-review

149 Scopus citations

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. 1C₅₀ 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.

Original language	English
Pages (from-to)	151-155
Number of pages	5
Journal	BioFactors
Volume	12
Issue number	1-4
DOIs	https://doi.org/10.1002/biof.5520120124
State	Published - 2000

Keywords

Anticancer
Peptide
Soy protein
Thermoase hydrolyzates

UN SDGs

This output contributes to the following UN Sustainable Development Goals (SDGs)

Access to Document

10.1002/biof.5520120124

Cite this

@article{1db951cd13d242d7b0a24d75e7018ba9,

title = "Anticancer activity of hydrophobic peptides from soy proteins",

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. 1C50 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, Soy protein, Thermoase hydrolyzates",

author = "Kim, \{Song E.\} and Kim, \{Hyuck Hwa\} and Kim, \{Ji Yeon\} and Kang, \{Young Im\} and Woo, \{Hee Jong\} and Lee, \{Hyong Joo\}",

year = "2000",

doi = "10.1002/biof.5520120124",

language = "English",

volume = "12",

pages = "151--155",

journal = "BioFactors",

issn = "0951-6433",

number = "1-4",

}

TY - JOUR

T1 - Anticancer activity of hydrophobic peptides from soy proteins

AU - Kim, Song E.

AU - Kim, Hyuck Hwa

AU - Kim, Ji Yeon

AU - Kang, Young Im

AU - Woo, Hee Jong

AU - Lee, Hyong Joo

PY - 2000

Y1 - 2000

N2 - 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. 1C50 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.

AB - 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. 1C50 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.

KW - Anticancer

KW - Peptide

KW - Soy protein

KW - Thermoase hydrolyzates

UR - http://www.scopus.com/inward/record.url?scp=0034490832&partnerID=8YFLogxK

U2 - 10.1002/biof.5520120124

DO - 10.1002/biof.5520120124

M3 - Article

C2 - 11216478

AN - SCOPUS:0034490832

SN - 0951-6433

VL - 12

SP - 151

EP - 155

JO - BioFactors

JF - BioFactors

IS - 1-4

ER -

Anticancer activity of hydrophobic peptides from soy proteins

Abstract

Keywords

UN SDGs

Access to Document

Other files and links

Fingerprint

Cite this