What if some of the most important scientific discoveries are already hidden in data collected years ago? Researchers at Tohoku University are exploring how AI and data-driven science can reveal new insights from past experiments and scientific literature. Their review highlights how old data could help accelerate discoveries in chemistry and materials science. 

Mechanochemistry is a growing field for chemical reactions that proceed in the solid state in the absence, or with miniscule amounts, of solvent added. For decades, solvents have been considered conventional for the progression of modern chemistry, nonetheless, researchers are increasingly demonstrating that mechanochemistry can synthesize complex molecules more effectively. With more progress, mechanochemistry could alleviate solvent-related environmental and financial burdens in chemical industries. New research from WPI-ITbM at Nagoya University demonstrates a simple mechanochemical method for synthesizing a series of synthetically challenging conductive organic molecules.

A joint research group consisting of Hikaru Ichida, a doctoral student in the Division of Nano Life Science, Graduate School of Frontier Science Initiative, Kanazawa University; Kosuke Mizuno, currently a Postdoctoral Researcher at the Institute for Protein Research, The University of Osaka; Professor Noriyuki Kodera and Associate Professor Holger Flechsig of the Nano Life Science Institute (WPI-NanoLSI), Kanazawa University; and Associate Professor Satoshi Toda of the Institute for Protein Research, The University of Osaka, has succeeded in visualizing the structural dynamics underlying how the serum protein Afamin stabilizes and transports Wnt3a, a lipid-modified signaling molecule. The study also showed that stable binding between these two molecules depends on both a hydrophobic pocket that accommodates Wnt3a and the structural integrity of Afamin. Wnt proteins are essential molecules that help the body develop properly and maintain healthy tissues. However, because they do not dissolve well in water and are highly hydrophobic, they tend to be unstable in the body. This study has revealed part of the mechanism by which Wnt3a is stably transported with the help of another protein. These findings are expected to deepen our understanding of biological processes involving Wnt3a and may contribute in the future to the development of ex vivo tissue engineering technologies and regenerative medicine.