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Peptide libraries displayed on bacteriophage

Erkki Koivunen, Ph. D.

Department of Biosciences
Division of Biochemistry
Phone: 708 595 54
Fax: 708 59068

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

Selected publications

Pasqualini, R., Koivunen, E., and Ruoslahti, E. av integrins as receptors for tumor targeting by circulating ligands. Nature Biotechnol. 15: 542-546, 1997.

Pulli, T., Koivunen, E., and Hyypiä, T. Cell surface interactions of Echovirus 22. J. Biol. Chem. 272: 21176-21180, 1997.

Sorsa, T., Salo, T., Koivunen, E. et al. Activation of type IV procollagenases by human tumor-associated trypsin-2. J. Biol. Chem. 272: 21067-21074, 1997.

Pasqualini, R., Bourdoulous, S., Koivunen, E. et al. A polymeric form of fibronectin has anti-metastatic effects on multiple tumor types. Nature Med. 2: 1197-1203, 1996.

Koivunen, E., Wang, B., and Ruoslahti, E. Phage libraries displaying cyclic peptides with different ring sizes: ligand specificities of the RGD-directed integrins. Bio/Technology 13: 265-270, 1995.

Pasqualini, R., Koivunen, E., and Ruoslahti, E. A peptide isolated from phage display libraries is a structural and functional mimic of an RGD-binding site on integrins. J. Cell Biol. 130: 1189-1196, 1995.

Koivunen, E., Wang, B., Dickinson, C. D., and Ruoslahti, E. Peptides in cell adhesion research. Methods Enzymol. 245: 346-369, 1994.

Koivunen, E., Wang, B., and Ruoslahti, E. Isolation of a highly specific ligand for the a5b1 integrin from a phage display library. J. Cell Biol. 124: 373-380, 1994.

Koivunen, E., Gay, D. A., and Ruoslahti, E. Selection of peptides binding to the a5b1 integrin from phage display library. J. Biol. Chem. 268: 20205-20210, 1993.


Finnish Cancer Society, Technology Development Centre (TEKES)

Last update 01.07.1998 Maintained by Jari Ylänne (