A chimera of a gelatinase inhibitor peptide with streptavidin as a bifunctional tumor targeting reagent.
A chimeric protein, consisting of streptavidin fused to a cyclic decapeptide with potent inhibitory activity for matrix metalloproteinases (MMP), has been produced in Escherichia coli and purified. The purified chimera formed a tetramer and showed full biotin-binding ability. The chimera was also capable of both binding to MMP-2 and inhibiting its activity. Thus, both the streptavidin moiety and the decapeptide of the chimera are fully functional. This bifunctional nature of the chimera should facilitate the application of the decapeptide since the streptavidin moiety can be used as a specific conjugation site for almost any materials upon biotinylation.
Farlow
Samuel J
SJ
Center for Molecular Imaging Diagnosis and Therapy and Basic Science Laboratory, Department of Radiology, Beth Israel Deaconess Medical Center, Harvard Medical School, 77 Avenue Louis Pasteur, Boston, MA 02115, USA.
Wang
Ruo Jie
RJ
Pandori
Mark W
MW
Sano
Takeshi
T
D000595:Amino Acid Sequence; D006801:Humans; D061965:Matrix Metalloproteinase Inhibitors; D009369:Neoplasms / Q000175:diagnosis; D009842:Oligopeptides / Q000737:chemistry; D011480:Protease Inhibitors / Q000737:chemistry; D011993:Recombinant Fusion Proteins / Q000737:chemistry; D019809:Streptavidin
D061965:Matrix Metalloproteinase Inhibitors; D009842:Oligopeptides; D011480:Protease Inhibitors; D011993:Recombinant Fusion Proteins; D019809:Streptavidin