ORGN 694 |
Peptide functionalized liposomes: A supramolecular approach to stabilize secondary structure
| Dennis W.P.M. Lowik1, Jan C. M. van Hest2, and Joris Meijer1. (1) Organic Chemistry, University of Nijmegen, Toernooiveld 1 - U177, 6525 ED Nijmegen, Netherlands, (2) Department of Organic Chemistry, Nijmegen University, Toernooiveld 1, 6525 ED Nijmegen, Netherlands |
A novel non-covalent approach to stabilize secondary structures of peptides is presented, employing a liposome bilayer as a scaffold. Oligopeptides capable of forming e.g. beta-hairpins or helices can be modified on both the N- and C-terminus with hydrophobic moieties, allowing the peptides to be anchored at both ends in the dynamic bilayer, as shown schematically below. Our synthetic strategy allows us to introduce a variety of N- and C-terminal hydrophobic modifications on any peptide entirely on the solid phase. This in our view simple approach, results in stabilization of the folding pattern without much interference with the dynamic character of the peptide, contrary to covalent methods used to impose secondary structure. Finally, modification of the liposome periphery by non-covalent interactions and exploiting the fluidic nature of the bilayer allows for the preparation of combinatorial libraries of epitopes that can be used to display discontinuous epitopes required for protein-protein interaction. |
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Proteins, Peptides, Amino Acids, and Nucleotides
8:30 AM-11:30 AM, Thursday, September 11, 2003 Sheraton New York -- Royal Ballroom B, Oral
Division of Organic Chemistry
The 226th ACS National Meeting, New York, NY, September 7-11, 2003
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