Chemistry
Functionalizing Fluorescent Proteins for the Detection of Explosive Materials in an Ultra-Sensitive Hydrogel-Based System
Document Type
Oral Presentation
Location
Indianapolis, IN
Start Date
10-4-2015 11:30 AM
End Date
10-4-2015 12:00 PM
Sponsor
Chad Wallace (Anderson University)
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.
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.