“This study showed that the synchrotron-radiation-based experimental technique could clearly monitor the alternations of structural components of the keratin protein under the conditions of heat damage, which is difficult by other methods,” Associate Professor Koichi Matsuo of HiSOR said. Before this, he explained that they could only see how the proteins look before they were heated and after thermal aggregation — not the process as it happens.

The progressive information on the protein’s structural changes will help their search for active ingredients that can suppress heat damage in hair. “Based on this research, we can develop new haircare products capable of curing or suppressing hair damage due to the heat treatment,” Matsuo said. “By monitoring protein’s structural changes, we could rapidly and accurately judge which ingredients can effectively inhibit the structural change of keratin proteins from various candidates of compounds,” he explained, adding that they could also get data such as the heatproof temperature for each active ingredient. The researchers hope their technique could also prove useful in studying other biological phenomena involving protein suspension or aggregation, such as Alzheimer’s disease.

“Our technique enables us to analyze the protein structures under various conditions, including physiological ones. The technique would also be useful for elucidating the structural alternation of other suspended or aggregated proteins such as amyloid fibrils and membrane-bound proteins, which is the cause of Alzheimer’s disease,” he said. They presented some of their research findings during the 20th annual meeting of the Protein Science Society of Japanheld last year.