ORGN 488 |
| Harvey R. Johnson1, Douglas S Clark1, and Matthew B. Francis2. (1) Department of Chemical Engineering, University of California, Berkeley, 743 Latimer Hall, Berkeley, CA 94720-1460, (2) Department of Chemistry, University of California, Berkeley, 724 Latimer Hall, Berkeley, CA 94720-1460 |
| The solubilization of bacteriophage MS2 in various organic solvents represents the first extraction of a capsid or comparably sized protein aggregate into any organic solvent. A coupling of a solvatochromic dye to the external face of MS2 was employed to elucidate the mechanism by which solubilization occurred: surfactant-protein pairing or reversed micelle incorporation of the capsid. It was determined that both mechanisms could occur depending on the amount of water present in the sample. At high surfactant concentrations, a continuum of solvation states best describes the local environment of the capsid. Modification of the protein assembly with a hydrophobic substrate was carried out in organic solvents to demonstrate that the range of synthetic reactions available for bioconjugation could be expanded using this technique. The solubilized capsid is also under investigation as a stable, robust template for polymerization reactions from its internal and external surfaces. |
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Total Synthesis, Asymmetric Reactions and Syntheses, Bioorganic
9:00 AM-11:00 AM, Wednesday, March 31, 2004 Anaheim Convention Center -- Hall C, Poster
Division of Organic Chemistry |