Detection of antimicrobial peptide-based universal detection system of enzyme activities and its application to theranostics

2014 Fiscal Year Final Research Report

• Project/Area Number: 24651259
• Research Category: Grant-in-Aid for Challenging Exploratory Research
• Allocation Type: Multi-year Fund
• Research Field: Chemical biology
• Research Institution: Osaka University
• Principal Investigator: MIZUKAMI Shin 大阪大学, 工学(系)研究科(研究院), 准教授 (30420433)
• Project Period (FY): 2012-04-01 – 2015-03-31
• Keywords: 抗菌ペプチド / 蛍光 / 酵素活性

Outline of Final Research Achievements

So far, we had developed a light-responsive compound release system by designing a functional antimicrobial peptide, temporin L (TL), modified with a photo-responsive protective group and combining liposomes including fluorophores. In this study, we newly developed an enzyme-responsive compound release system by making fusion peptides of TL and enzyme substrates. We chose caspase-3 and phosphatases as the target enzymes. For caspase-3, the enzyme substrate peptide was modified to the ε-amino group to yield a branched peptide. For phosphatases, a phosphorylated amino acid was substituted with one of the amino acids in TL. In both cases, the target enzyme activity activated the membrane-damaging activity of the fusion peptides. By using liposome including fluorophores, the system was applied to fluorescence detection of the target enzymes.

Free Research Field

ケミカルバイオロジー