Serum albumin, gene delivery

Rhaese, S., von Briesen, FI., Rubsamen-Waigmann, FI., Kreuter, J., and Langer, K. (2003), Human serum albumin-polyethylenimine nanoparticles for gene delivery, J. Controlled Release, 92(1-2), 199-208. 

Polycationic Serum Albumin Proteins for Gene Delivery. 218... 

Fig. 4 Top Cationization of the protein human serum albumin carrying multiple positively charged primary amino groups. Images show that such albumin polycations (stained red) reveal efficient cellular uptake by clathrin-mediated endocytosis, endosomal release (yellow arrows), and allow gene delivery and release into cells due to tight interaction of DNA, as exemplified by the isothermal titration calorimetry graph...

Serum albumin has also been tested as NPs for gene delivery. Mo et al. [88] encapsulated the DNA into human serum albumin (HSA) by a desolvationcrosslinking method to produce DNA-HSA NPs having a mean size of 120 nm and zeta potential of —44 mV. The DNA-HSA NPs were easily taken up by the cells via receptor-mediated endocytosis that involved primarily caveolae pathways. Within the cells, DNA-HSA NPs protected the DNA against nuclease attack and showed sustained release of DNA over 6 days without significant cytotoxicity. The overall transfection rate was found to be fivefold higher than obtained with Lipofectamine. 

Mo Y, Barnett ME, Takemoto D et al (2007) Human serum albumin nanoparticles fw efficient delivery of Cu, Zn superoxide dismutase gene. Mol Vis 13 746-757... 

Fischer, D., Bieber, T., Brusselbach, S., etal. (2001) Cationized human serum albumin as anon-viral vector system for gene delivery Characterization of complex formation with plasmid DNA and transfection efficiency, Int. J. Pharm., 225, 97-111. 

Although gene manipulation techniques offer the possibility of making recombinant human serum albumin (rHSA) [94], numerous studies have used bovine serum albumin (BSA) in the development of drug delivery systems, more due to the economic factor than to the chemical differences between HSA and BSA. Both proteins have similar folding and a well-known primary structure the most notable difference is the presence of two tryptophan residues in bovine albumin, while human albumin has a unique tryptophan [95]. 

Mo, Y. and M.E. Barnett, Human serum albumin nanoparticles for efficient delivery of Cu,Zn superoxide dismutcise gene. Molecular Vision, 13 746-757, 2007. 

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