Proper protein-protein interactions are instrumental to the functionality of an organism. The study of whether or not proteins are able to fold and interact appropriately has been widely recognized as one of the most important ways we can learn, treat, and prevent diseases like tumorigenesis and Alzheimer’s which are caused by misfolded protein or unfavorable interaction with foreign inhibitors. Although methods exist for investigating the nature of protein structure and interaction, many require advanced training, highly specialized equipment, and are conducted under non-native protein conditions. A rapid, easy to use, and affordable screening method is the most ideal for preliminary testing of protein structural change, acting as a pre-screen of potential interaction pairs prior to more advanced experimental methods. Fluorescamine is a fluorogenic dye that interacts with primary amine groups present on amino acids. This compound selectively targets solvent-accessible amines, making it useful for monitoring protein conformational changes and protein-protein interactions. The purpose of this project is to establish the effectiveness of the fluorescamine assay as a high throughput method for the screening of protein-protein interactions. Several well-characterized protein pairs, such as gc-globulin and actin, were used in a case study to confirm the validity of this screening method. Through a combination of fluorescamine tagging to validate the existence of an interaction pair, as well as mass spectrometry to identify the location of tagging, the protein-protein interaction interfaces can be identified.

Determining protein tertiary structure and protein-protein interaction interfaces via fluorescamine tagging of surface amines

Macromolecular Chemistry: The Second Century

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ACS Spring 2020 National Meeting & Expo

The official archive and repository for all ACS Meetings & Expositions abstracts and select posters or presentations.