Preparation and functional evaluation of RGD-modified streptavidin targeting to integrin-expressing melanoma cells

Syrkina, M.S.; Shirokov, D.A.; Rubtsov, M.A.; Kadyrova, E.L.; Veiko, V.P.; Manuvera, V.A.

Авторы: Syrkina Marina S., Shirokov Dmitry A., Rubtsov Mikhail A., Kadyrova Elena L., Veiko Vladimir P., Manuvera Valentin A.
Журнал: Protein Engineering, Design and Selection
Том: 26
Номер: 2
Год издания: 2013
Издательство: Oxford University Press
Местоположение издательства: United Kingdom
Первая страница: 143
Последняя страница: 150
DOI: 10.1093/protein/gzs076
Аннотация: The vertical growth stage is the most dangerous stage of melanoma and is often associated with a poor prognosis. The increased invasiveness and metastasis that is typical for vertically growing melanoma are mediated by the molecules of cell adhesion (particularly, integrins). Integrin v3, which is abundantly expressed on melanoma cells with high metastatic potentials and is characterized by low expression levels in normal melanocytes, is potentially an attractive target for melanoma diagnostics and therapy. Integrin v3 is known to recognize the arginine-glycine-aspartic (RGD) sequence, which has been found in a wide variety of its natural ligands. Here expression vectors bearing the genes of fusion proteins have been constructed for producing these proteins in Escherichia coli. Such fusion proteins consist of a peptidic oaddress,' targeting the integrins on melanoma cells, linked to an oadaptor' for the attachment of a diagnostic or toxic agent. The peptidic oaddress' contains the RGD motif, which is stabilized by a disulfide bond to achieve the optimal receptor binding conformation. The oadaptor' is a tetrameric protein, namely, streptavidin, that is able to achieve high-affinity binding of d-biotin (K-d 10(15) M) and confer avidity to the address peptide. This binding ability facilitates the generation of anti-melanoma diagnostic and therapeutic agents using the appropriate biotin derivatives. These recombinant proteins were purified from the periplasm of E.coli using columns with 2-iminobiotin agarose and demonstrated an ability to adhere to the surface of murine and human melanoma cells.
Добавил в систему: Рубцов Михаил Александрович

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Preparation and functional evaluation of RGD-modified streptavidin targeting to integrin-expressing melanoma cellsстатья

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