MEDI 12 |
| To better understand and control β-sheet interactions between disease-related proteins, our research group is developing chemical models of protein β-sheets. Recently, we developed 54-membered-ring cyclic peptides that mimic protein quaternary β-sheet structure in water through interchain β-sheet interactions. These cyclic peptides, which contain the unnatural amino acid Hao on one edge and a heptapeptide β-strand on the other edge, form β-sheet dimers that further associate to form tetrameric β-sheet sandwiches. This paper describes two ongoing studies of the interaction between these peptides and β-sheet peptides and proteins. The first focuses on inhibiting β-amyloid formation with cyclic peptides containing complementary heptapeptide β-strands. The second focuses on binding a soluble protein (a protein G variant) with a cyclic peptide containing a complementary heptapeptide β-strand.
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Medicinal Chemistry Award Symposium
1:30 PM-4:20 PM, Sunday, August 19, 2007 BCEC -- 210B, Oral
Division of Medicinal Chemistry |
