Attenuating the expression of HIF-1α
(hypoxic inducible factor)
by siRNA has an effect on the proliferation of hypoxia cancers. Mitochondria
targeting siRNA may silence the level of HIF-1α for cancer gene
therapy. A GAG-rich DNA was conjugated to GC-rich DNA for the synthesis
of functional magnetic nanoaptamer (DNA-Fe3O4) to keep the innate character of the targeting aptamer. The DNA-Fe3O4 can load the hydrophobic dye (BODIPY-OCH3) by the GC-rich sequences, resulting in fluorescent nanoaptamer
(BFe@DNA). Self-assembly of BFe@DNA with target aptamer resulted in
the formation of BFe@DNAH. Subcellular fluorescence imaging
results confirm that BFe@DNAH can accumulate in MCF-7 cells
and selectively target mitochondrion. In particular, BFe@DNAH can transport siRNA to breast cancer cells or tissues for the attenuation
of HIF-1α and ATP and the inhibition on growth of cancer cells
in vivo. Therefore, BFe@DNAH is a smart nanoaptamer platform
for the development of subcellular imaging agents and gene therapy.
Microbe-catalyzed surface modification is a promising method for the production of special targeting nanomaterials. A bacterium-selective material can be obtained by investigating the microbe-catalyzed mineralization of proteins. Herein, a novel method was fabricated for the biosynthesis of FeS-decorated porphyrin−protein clusters (P-CA@BE) via E. coli (Escherichia coli)catalyzed bio-Fe(III) reduction and bio-sulfidation of porphyrin (P), caffeic acid (CA), and protein [bovine serum albumin (BSA)] assemblies. The assembly (P-CA@BSA) was identified by spectroscopic methods. Next, the P-CA@BSA assembly was transferred into FeS-decorated porphyrin−protein clusters (P-CA@BE) catalyzed by E. coli. There are partial β-folding proteins in P-CA@BE, which selectively recognize S. aureus (Staphylococcus aureus) and show different antibacterial properties against E. coli and S. aureus. Results demonstrate that the E. coli-catalyzed mineralization of the porphyrin−protein assembly is an effective method for the biosynthesis of S. aureus-sensitive metal−protein clusters.
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