CHED 513 |
| Basic region leucine zipper (bZip) proteins such as the yeast transcription activator GCN4 contain a bipartite DNA-binding motif consisting of a coiled-coil leucine zipper dimerization domain and a highly charged basic region that directly contacts DNA. The monomeric basic region appears to be unfolded in the absence of DNA, but assumes a helical structure upon sequence-specific binding as a homodimer to a DNA recognition site. Replacement of the leucine zipper region by a disulfide bond at the C-terminus leads to peptides which maintain their sequence specificity recognizing both AP-1 (ATGAcTCAT) and CRE (ATGAcgTCAT) sites with high affinity at 4 ºC. In order to extend the reach of this work, we have envisioned synthetic mini-proteins in which dimerization can be facilitated by the use of a 1,3-dipolar cycloaddition (Click) reaction. Herein, we report the development of site-switchable DNA-binding peptides which have been modified with alkyne or azide containing amino acids at the C-terminus of the mini-protein. The alkyne or azide groups can be exploited in a late-stage 1,3-dipolar cycloaddition reaction as the critical step leading to artificial dimerization. |
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Undergraduate Research Poster Session: Organic Chemistry
11:00 AM-1:00 PM, Monday, April 7, 2008 Morial Convention Center -- Hall A, Poster
Division of Chemical Education |