Cryo-EM is changed to be useful method for medical and pharmaceutical applications

Cryo-EM for medical and pharmaceutical studies

11:45-12:15

【Profile】

Yoshinori Fujiyoshi was born in Gifu, Japan, in 1948, and graduated from the Faculty of Science, Nagoya University in 1971. He received his Ph.D. from Kyoto University in 1982. In 1980, he began working as a Research Assistant at the Institute for Chemical Research, Kyoto University. He then moved to the Protein Engineering Research Institute as a Senior Research Scientist and Research Director in 1987 and 1988, respectively. After 1994, he was the Research Director at the International Institute for Advanced Research, Matsushita Electric Industrial Co., Ltd. In 1996, he became a Professor at the Graduate School of Science, Kyoto University. He moved to Nagoya University in 2012. He then became a Distinguished Professor at TMDU Advanced Research Institute, Tokyo Medical and Dental University in 2019. He founded a business venture company, CeSPIA Inc. By developing cryo-electron microscopes, he has focused his efforts on the high-resolution analysis of the structures of membrane proteins, such as water channels, ion channels, receptors, gap junction channels, and tight junctions, to better understand their physiological functions. The development of electron crystallography, single particle analysis and cryo-electron tomography together with continued instrument development will extend the ability of obtaining high-resolution information from increasingly complex protein-lipid structures and living organisms.

【Abstract】

Our structure analysis discriminated water molecules in the channel of AQP4 which is the predominant water channel in brain. We proposed a model for understanding mechanism of the water channel which excludes permeation of any ions and even protons keeping fast water transport. However, the necessity of crystallization makes this method less popular. By single particle analysis, many structures have recently been analysed. We analysed structures of some important proteins including gap junction channel in short period by this method. Structural biology enables us to analyse structures of important target proteins in medical and pharmaceutical studies. For example, many lead compounds and target proteins have to be thrown into garbage owing to adverse effects. These could be rescued as a drug candidate by modifying the ligand chemicals on the ideal parts for pharmacologic actions and reducing the adverse effects based on structural information.

Molecular mechanism of membrane proteins based on the Cryo-EM structures towards medicinal application

12:15-12:45