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A chimera of a gelatinase inhibitor peptide with streptavidin as a bifunctional tumor targeting reagent
Author(s) -
Farlow Samuel J.,
Wang Ruo Jie,
Pandori Mark W.,
Sano Takeshi
Publication year - 2002
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(02)02565-6
Subject(s) - chimera (genetics) , streptavidin , chemistry , biotinylation , bifunctional , tetramer , fusion protein , peptide , biochemistry , moiety , microbiology and biotechnology , biotin , stereochemistry , recombinant dna , enzyme , biology , gene , catalysis
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.