CHED 564 |
| This study looked at the photophysical interaction of porphyrin probes with a protein solution. The data shows that the structure of the porphyrin probe affects the ability of the probe to interact with the host protein. Various spectral and kinetic experiments (including lifetimes, Stern-Volmer constants and spectral studies) are presented to characterize the host-guest interaction between porphyrins and the human serum albumin (HSA) protein system. Further, self-quenching experiments were conducted on each of the probes to determine if porphyrin aggregation is a problem at the concentrations being studied. Data has been collected for protoporphyrin IX (PPIX), hematoporphyrin (Hme), the diesters of PPIX and Hme, chlorine e6 (Ce6), deuteroporphyrin IX 2,4 bis ethylene glycol (DPIX), and octaethylporphine (OP) in homogeneous solvents, buffer, and HSA protein solutions. The data shows that the interaction of porphyrin and protein varies as the structure of the porphyrin is altered. |
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Undergraduate Research Poster Session: Organic Chemistry
11:00 AM-1:00 PM, Monday, March 26, 2007 Hyatt Regency Chicago -- Riverside Center, Poster
Division of Chemical Education |