CHED 791 |
| Catherine L. Thomas1, Marcus A. Etienne1, Jia Wang1, Vladimir Setnicka2, Timothy A. Keiderling2, and Robert P. Hammer1. (1) Department of Chemistry, Louisiana State University, 232 Choppin Hall, Baton Rouge, LA 70803, (2) Department of Chemistry, University of Illinois at Chicago, Chicago, IL 60607 |
| There are a number of diseases that are caused by the misfolding of proteins into fibrils, which consist of predominantly β-sheet secondary structure. Recently several groups have succeeded in making autonomously folding β-hairpin peptides, which serve as excellent models for studying β-sheet structure. A key discovery in making stable β-hairpin peptides was that DPro-Gly and Asn-Gly sequences form type-II’ and type-I’ β-turns respectively. Our group is studying the role that α,α-disubstituted amino acids (ααAAs) can play in stabilizing both the turn and the sheet portion of β-hairpins. Several analogs of the Gellman peptide (Figure) have been prepared having Aib (R3, R4=CH3) or Dpg (R3,R4=propyl) in the i+1 position of the β-turn and various Α-amino acids in the i+2 position of the β-turn, including Gly, Ala, and DAla. Additionally ααAAs such as Dpg and Dibg (R1, R2=isobutyl) have been incorporated at position 3 of the β-hairpin. Conformational studies showing that ααAAs can greatly stabilize the secondary structure of β-hairpins will be presented.
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Undergraduate Research Poster Session: Organic Chemistry
2:00 PM-4:00 PM, Monday, March 29, 2004 Anaheim Convention Center -- Hall A, Poster
Division of Chemical Education |
