Structural Molecular Pharmacology Lab

AboutAbout the lab

Aiming at next-generation drug discovery guided by three-dimensional structure

The Structural Molecular Pharmacology Lab conducts research in drug discovery science using the three-dimensional structures of proteins and nucleic acids.
Two units work in close cooperation: a group that pursues structure-based drug discovery targeting proteins, and the Kodama Group, which pursues drug discovery using structurally controlled nucleic acids.
The main method used, nuclear magnetic resonance (NMR) spectroscopy, is well suited to determining the structures of small protein domains and to rapidly detecting their interactions with low-molecular-weight drugs.
On the lab's website, the lab is introduced as being able to cover everything from genome-based drug discovery to preclinical research within a single lab.

ResearchResearch themes

To understand life processes, it helps to examine the shapes of proteins, which are their building blocks. The lab mainly uses nuclear magnetic resonance (NMR) spectroscopy to study structures in aqueous solution and interactions with other molecules, and combines it with X-ray crystallography and cryo-electron microscopy.

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Drug discovery targeting tight junctions↗

The lab targets PDZ domain proteins, which serve as scaffolds for cell adhesion apparatuses such as epithelial tight junctions. It has determined the structures of several PDZ domains and has found compounds that strengthen tight junctions, as well as compounds that weaken them and open the barrier.

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Structurally controlled nucleic acid therapeutics↗

Non-natural oligonucleotides, in which the shape of the sugar moiety is fixed by chemical cross-linking, show better properties in vivo than ordinary nucleic acids. While studying their physical properties and thermodynamic stability, the lab aims to design and put into practical use antisense drugs, aptamer drugs, and others.

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Drug discovery targeting intrinsically disordered proteins↗

The lab found that intrinsically disordered proteins have cryoprotective and lyoprotective effects on other enzymes. It is currently pursuing drug discovery research targeting proteins involved in infectious diseases, as a participant in an AMED-CREST project and under the guidance of a professor at Niigata University.

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Aggregates of the tumor suppressor protein p53↗

p53 is one of the tumor suppressors found mutated in about half of all cancers. When only one copy of the gene is mutated, even the product of the normal copy becomes inactive. The lab hypothesizes that the diverse aggregates formed by p53 are involved in this phenomenon, and conducts physicochemical studies on the formation and detection of oligomers.

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