Chemistry

Functionalizing Fluorescent Proteins for the Detection of Explosive Materials in an Ultra-Sensitive Hydrogel-Based System

Presenter Information

Ethan Hillman, Anderson University

Document Type

Oral Presentation

Location

Indianapolis, IN

Start Date

10-4-2015 11:30 AM

End Date

10-4-2015 12:00 PM

Description

Detecting explosive material is a great concern of national security; improving the sensitivity with which these materials are detected is crucial for increased safety. Fluorescent proteins are known to emit photons with wavelengths which are very specific to that particular protein. These wavelengths are highly specific because they are governed by interactions within the protein's structure. These interactions are sensitive to the point that even a slight change in the conformation of the protein could affect this emitted wavelength. Therefore, proteins which are sensitive to aromatic compounds would undergo a conformational change in the presence of an explosive, and thus cause a change in the emitted wavelength of the fluorescent protein. Based on this premise, fluorescent proteins expressed by modified E. coli were extracted, modified by a reaction with o-mesitylsulfonylhydroxylamine (MSH), and incorporated into a polyacrylamide gel. Gels were then evaluated based upon their electrophoretic properties. The MSH synthesis has been confirmed; however, pure product has never been used in the modification reaction before it decomposed. At present, the gels have shown no sign of protein incorporation or modification.

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Apr 10th, 11:30 AM Apr 10th, 12:00 PM

Functionalizing Fluorescent Proteins for the Detection of Explosive Materials in an Ultra-Sensitive Hydrogel-Based System

Indianapolis, IN

Detecting explosive material is a great concern of national security; improving the sensitivity with which these materials are detected is crucial for increased safety. Fluorescent proteins are known to emit photons with wavelengths which are very specific to that particular protein. These wavelengths are highly specific because they are governed by interactions within the protein's structure. These interactions are sensitive to the point that even a slight change in the conformation of the protein could affect this emitted wavelength. Therefore, proteins which are sensitive to aromatic compounds would undergo a conformational change in the presence of an explosive, and thus cause a change in the emitted wavelength of the fluorescent protein. Based on this premise, fluorescent proteins expressed by modified E. coli were extracted, modified by a reaction with o-mesitylsulfonylhydroxylamine (MSH), and incorporated into a polyacrylamide gel. Gels were then evaluated based upon their electrophoretic properties. The MSH synthesis has been confirmed; however, pure product has never been used in the modification reaction before it decomposed. At present, the gels have shown no sign of protein incorporation or modification.