Alanyzing the substrate multispecificity of human peptide transporter
Project/Area Number |
26702002
|
Research Category |
Grant-in-Aid for Young Scientists (A)
|
Allocation Type | Partial Multi-year Fund |
Research Field |
Eating habits
|
Research Institution | University of Shizuoka |
Principal Investigator |
Ito Keisuke 静岡県立大学, 食品栄養科学部, 准教授 (40580460)
|
Project Period (FY) |
2014-04-01 – 2017-03-31
|
Project Status |
Completed (Fiscal Year 2016)
|
Budget Amount *help |
¥16,120,000 (Direct Cost: ¥12,400,000、Indirect Cost: ¥3,720,000)
Fiscal Year 2016: ¥2,080,000 (Direct Cost: ¥1,600,000、Indirect Cost: ¥480,000)
Fiscal Year 2015: ¥2,600,000 (Direct Cost: ¥2,000,000、Indirect Cost: ¥600,000)
Fiscal Year 2014: ¥11,440,000 (Direct Cost: ¥8,800,000、Indirect Cost: ¥2,640,000)
|
Keywords | ペプチド輸送体 / 必須アミノ酸 / 食品 / 生体機能利用 / ペプチド / ペプチド栄養 / 分岐鎖アミノ酸 / 芳香族アミノ酸 / 機能性ペプチド / トランスポーター / 機能性食品 / ハイスループットスクリーニング / Saccharomyces cerevisiae / 食品成分の吸収 / ジペプチド |
Outline of Final Research Achievements |
Proton-coupled oligopeptide transporter (POT) family proteins are characterized by their substrate multispecificity that one transporter can recognize as many as 8,400 types of di/tripeptides as substrates. This unique characteristic enables certain types of drugs to be absorbed by the human intestine and kidney. In this study, we elucidated the substrate multispecificity of human PEPT2 by the comprehensive analysis using a dipeptide library. Dipeptides that comprised aromatic amino acids and branched-chain amino acids displayed high-affinity for hPEPT2. The biosynthesis of aromatic amino acids and branched-chain amino acids requires the expression of multiple enzymes and involves energy-consuming reactions. Therefore, the substrate multispecificity of hPEPT2 is suitable to import the high-value amino acids.
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Report
(4 results)
Research Products
(19 results)