2013 Fiscal Year Final Research Report
Identification, exhaustive analysis, clarification of action mechanism and efficient modification of novel hypolipidemic peptides
| Project/Area Number |
23380075
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| Research Category |
Grant-in-Aid for Scientific Research (B)
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| Allocation Type | Single-year Grants |
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| Section | 一般 |
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| Research Field |
Food science
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| Research Institution | Gifu University |
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Principal Investigator |
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| Co-Investigator(Kenkyū-buntansha) |
HONDA Hiroyuki 名古屋大学, 大学院・工学系研究科, 教授 (70209328)
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| Project Period (FY) |
2011-04-01 – 2014-03-31
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| Keywords | コレステロール / ペプチド / ミセル / ペプチドアレイ / 胆汁酸 / 食品機能 / ABCA1 / ラクトスタチン |
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| Research Abstract |
We used the luciferase plasmid containing the cholesterol transporter, intestinal ABCA1 gene promoter to clarify the molecular mechanism of the inhibition of intestinal cholesterol absorption by lactostatin in Caco-2 cells. Our results suggested that PPAR/LXR responsive element related to the suppression of cholesterol absorption by lactostatin in Caco-2 cells. An oleosin having a hypocholesterolemic action was investigated to clarify the active sequence of its induced a hypocholesterolemic action by an exhaustive analysis using a peptide array. We found two novel bile acid binding peptides. Two novel bile acid binding peptides exhibited the greater inhibition of micellar solubility of cholesterol in vitro compared with a bile acid binding peptide VAWWMY as a positive control. We found that QEK derived from soybean beta-conglycinin alpha prime subunit exhibited the significant increase in CYP7A1 mRNA levels compared to the control group in HepG2 cells.
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[Journal Article] Screening of peptides with a high affinity to bile acids using peptide arrays and a computational analysis2011
Author(s)
Takeshita, T., Okochi, M., Kato, R., Kaga, C., Tomita, Y., Nagaoka, S. and Honda, H
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Journal Title
J. Biosci. Bioeng
Volume: 112
Pages: 92-97
Peer Reviewed
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