Structural analysis of protein using synchrotron-radiation vacuum-ultraviolet circular dichroism and study of biomolecular interactions

2017 Fiscal Year Final Research Report

• Project/Area Number: 15K07028
• Research Category: Grant-in-Aid for Scientific Research (C)
• Allocation Type: Multi-year Fund
• Section: 一般
• Research Field: Biophysics
• Research Institution: Hiroshima University
• Principal Investigator: Matsuo Koichi 広島大学, 放射光科学研究センター, 准教授 (40403620)
• Project Period (FY): 2015-04-01 – 2018-03-31
• Keywords: 円二色性 / 放射光 / 真空紫外線 / 生体膜 / 蛋白質 / 二次構造

Outline of Final Research Achievements

We developed new analytical method which can characterize the structure of membrane-bound protein using vacuum-ultraviolet circular-dichroism (VUVCD) and linear-dichroism (LD) spectroscopy. This VUVCD-LD method uses the flow-LD measurement system equipped with the microchannel type flow cell and liquid pump, and can analyze the orientation of secondary structures at the local region such as membrane binding site of protein. This system was applied to the structural analysis of alpha1-acid glycoprotein (AGP) and myelin-basic protein (MBP) in the membrane. It is known that AGP transports a drug into membrane and MBP relates to the myelination in nerve cell. The secondary structures of AGP and MBP were determined by VUVCD-LD method in the presecne of various liposomes, revealing that the drug-binding regions of AGP directly interacted with membrane and that the driving force of MBP-membrane binding was electrostatic interaction.

Free Research Field

生物物理化学