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Tohoku University Technology: Visualization Probe for Protein Denaturation: T21-051

A method for chemically labeling denatured regions of proteins.

To visualize protein denaturation, conventional methods have developed chemical probes that bind to denatured regions of proteins, resulting in increased fluorescence intensity. However, the binding between conventional fluorescent probes and denatured protein regions has been reversible. Therefore, in mixed protein systems, it has been difficult to link which protein's denaturation is causing the increase in fluorescence intensity. The fluorescent probe invented by Dr. Shinichi Sato and colleagues at the Interdisciplinary Research Institute for Frontier Science distinguishes itself from conventional denatured protein probes by forming a direct covalent bond with the denatured and aggregated sites of proteins. Additionally, it is a non-fluorescent molecule before the reaction and exhibits fluorescence only when it forms a covalent bond with aggregated proteins. Approximately 30 types of probes with varying detection sensitivities for denaturation have been developed so far. Furthermore, there are innovations that allow for the concentration of denatured and aggregated proteins, as well as their peptide fragments, enabling mass spectrometry analysis of only the proteins that reacted with the probe.

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