A new biotin labeling agent that allows control over the introduction location and quantity [Saitama University]

Re-crosslinking of S-S bases is the key! A novel biotin labeling agent that stabilizes the structure and function of proteins.

Conventional biotin labeling randomly binds to functional groups of proteins, making it difficult to control the number of biotins bound and their binding positions. Additionally, the cleaved S-S bonds for labeling do not re-bridge, which poses a challenge as it can lead to changes in the higher-order structure of the protein and a decrease in activity. In this technology, biotin is introduced to the Br group of dibromo-pyridazine dione, and the re-bridging of S-S bonds occurs simultaneously with labeling. This stabilizes the higher-order structure of the protein and preserves its activity. The number of bound biotins can be selected as either one or two, and it can be used for controlling the orientation of proteins by utilizing the binding characteristics with streptavidin.

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