|Peptide libraries displayed on
We have constructed a series of random peptide libraries that are displayed on the surface of bacteriophage fuse 5. Peptides that bind to target molecules can be isolated from such libraries using biopanning selection. The size of the peptide insert in the libraries ranges from five to twenty variable amino acid residues. A cysteine pair has been included in some displayed peptides to constrain conformation of the peptides. Phage peptide libraries have been used in various applications, e.g. to find ligands to cell surface integrins, and to develop selective inhibitors to proteolytic enzymes. Peptides isolated with this stategy could be useful lead coumpounds to develop drugs to block the target molecules. The most active peptide we have developed so far is a a novel cyclic ten-residue peptide that inhibits specifically type IV collagenases /gelatinases and blocks cell migration in vitro and tumor invasion in vivo. To make peptide discovery faster and to increase the diversity of peptide libraries, we are also developing alternative genetic display strategies for degenerate peptides.
Johanna Lahdenranta, predoctoral student; Seija Taube, Licenciate of Dentistry
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Finnish Cancer Society, Technology Development Centre (TEKES)
|Last update 01.07.1998||Maintained by Jari Ylänne (email@example.com)|