ORGN 241 |
| Dieter Seebach, Department of Chemistry and Applied Biosciences, Department of Chemistry and Applied Biosciences, Laboratory of Organic Chemistry ETH Zuerich, Wolfgang-Pauli-Str. 10, HCI H331, Zuerich, 8093, Switzerland |
| Insertion of one or two CH2 groups in each amino acid residue of peptides leads to β- and γ-peptides of most exceptional properties. They form secondary structures in solution, such as helices, turns, and pleated sheets, with as few as four residues, they are entirely stable to the action of peptidases, they are metabolically stable in mammals, insects and plants, and they are hardly biodegradable. Still, small β- and γ-peptides can mimick α-peptidic hormones and other ligands in their interactions with proteins (receptors). These features make the peptides built from homologated proteinogenic amino acids promising candidates for diagnostic and pharmaceutical applications. In the lecture a review will be given of the results, obtained since the beginning, eight years ago, of the journey into the world of β-peptides. Results of the newest investigations will be described; they include (i) β-amino acids with α-hydroxy, α-fluoro, and α-methylen substituents, and with a β-aza-insertion, (ii) Zn2+-binding β-peptides with Cys and His side chains (iii) thioligation with formation of long-chain β2- and β3-peptides, (iv) binding to DNA duplexes and (v) penetration into mammalian cells and lodging to nucleoli. For a current list of references to our papers on β- and γ-amino acids and –peptides see http://infosee.ethz.ch/seebach/research.html. |
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Tetrahedron Prize for Creativity in Organic Chemistry
1:00 PM-5:10 PM, Monday, August 23, 2004 Pennsylvania Convention Center -- Ballroom B, Oral
Division of Organic Chemistry |