Alanyzing the substrate multispecificity of human peptide transporter

2016 Fiscal Year Final Research Report

• 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
• Keywords: ペプチド輸送体

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.

Free Research Field

食品機能開発化学