ORGN 495 |
| Margaret A. Schmitt, Ahlke Hayen, and Samuel H. Gellman. Dept. of Chemistry, University of Wisconsin, 1101 University Ave., Madison, WI 53706 |
| Oligomers that adopt predictable conformations (“foldamers”) are subjects of increasing interest. Most foldamers reported to date have homogeneous backbones. We show that combining a-amino acid and cyclic b-amino acid residues in a sequentially alternating pattern can lead to helix formation within relatively short heterooligomers. Structural data suggest that these foldamers have a "split personality," simultaneously populating two different helical conformations and displaying a length-dependent shift in the percentage of each conformation adopted. This behavior parallels closely the split personality observed among peptides composed exclusively of a-amino acid residues, which frequently populate both a- and 310-helical conformations in solution. The different monomer types in the heterogeneous backbone offer complementary benefits to these new foldamers: the b-residues provide conformational preorganization, while the a-residues allow introduction of specific sidechains at specific positions. |
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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 |