Teflon proteins: Modulating protein structure and stability using fluorous amino acids

FLUO 22

E. Neil G. Marsh, nmarsh@umich.edu1, Hwang-Yeol Lee2, and Lindsey M. Gottler, lgottler@umich.edu2. (1) Chemistry, University Of Michigan, 930 N. University Ave., Ann Arbor, MI 48105, (2) Department of Chemistry, University of Michigan, Ann Arbor, MI 48109
Fluorocarbons are a quintessentially man-made class of molecules – fluorine being nearly absent from biology – that possess novel and useful physicochemical properties, typified by the non-stick nature of Teflon. Replacing hydrophobic amino acid residues in proteins and peptides with extensively fluorinated analogs provides a way to modify their properties in a predictable manner. The possibilities include designing proteins with enhanced thermal and chemical stabilities and the design of novel protein:protein recognition elements mediated by fluorous contacts.
 

Nanostructured Fluorocarbons: Smart Tectons for Self-Assembly
2:00 PM-4:25 PM, Monday, August 20, 2007 BCEC -- 252B, Oral

Division of Fluorine Chemistry

The 234th ACS National Meeting, Boston, MA, August 19-23, 2007