Part:BBa_K3824000

1) Basic information Buforins, which house a helix-hinge-helix domain, kill a microorganism by entering the cell without membrane permeabilization and thus binding to nucleic acids. The proline hinge is crucial for the cell penetrating activity of buforins. Buforins also are known to possess anti-endotoxin and anticancer activities, thus making these peptides attractive reagents for pharmaceutical applications.

We modified buforin IIB peptide sequence to induce cancer cell death by delivering doxorubicin and siRNA.

2) Modify Buforin IIB peptide - Amino acid sequence modification

Buforin IIB: RAGLQFPVGRLLRRLLRRLLR (21 aa) (charge = +7)

Modified Version 1 (MV1): RAGLQFPVGRLLRRLLR (17 aa) (charge = +5)

Modified Version 2 (MV2): RAGLQFPVGRLLR (13 aa) (charge = +3)

further modification: FITC was added to the c-terminal of the peptide to analyze the intracellular distribution in cancer cells. doxorubicin was added to the c-terminal of the peptide to analyze the drug sensitivity of doxorubicin (chemotherapy drug)

3) Goal of this project:

(1) Which peptide version has low cell cytotoxicity? MV1-FITC and MV2-FITC

(2) Which peptide can specifically target cancer cells without harming normal cells? MV1-FITC

(3) Can MV1 form complex with siRNA targeting CYP1A1? Yes (MV1-FITC)

(4) Which is more efficient inducing cancer cell death? MV1-Doxorubicin with siRNA