ORGN 608 |
| Flavoenzymes catalyze a series of biological processes including electron transfer and signal transduction through redox modulation of a flavin cofactor (FMN or FAD). Non-covalent supramolecular interactions fine-tune the cofactor redox properties to generate specific enzymatic function and isolate the cofactor in a hydrophobic binding pocket. Previous synthetic models have provided a general understanding of the role of hydrogen bonding, pi-stacking, and donor atom pi interactions, but have failed to regenerate the specific microenvironment within the apoenzyme. We report two distinct approaches to mimic the biological environment of the flavin cofactor using either nanoparticle or polymeric scaffolds in aqueous media. First, we use cationic nanoparticles to electrostatically bind to FMN, resulting in high affinity and modulation of the FMN reduction potential. Second, we use a water soluble flavin polymer synthesized via ATRP that provides both a relative hydrophobic environment and redox modulation of the appended flavin unit typical of some flavoenzymes. |
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Molecular Recognition and Self-Assembly
1:00 PM-5:00 PM, Wednesday, March 28, 2007 McCormick Place Lakeside -- Room E352, Level 3, Oral
Division of Organic Chemistry |