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Protamine nanoparticles for improving shRNA-mediated anti-cancer effects.

Liu M, Feng B, Shi Y, Su C, Song H, Cheng W, Zhao L - Nanoscale Res Lett (2015)

Bottom Line: Protamine nanoparticles were designed by encapsulating small hairpin RNA (shRNA)-expressing plasmid DNA targeting the Bcl-2 gene (shBcl-2) to silence apoptosis-related Bcl-2 protein for improving the transfection efficiency and cytotoxicity in cancer therapy.Our findings demonstrated that the obtained protamine nanoparticles possessed excellent characterizations of small particle size, homogenous distribution, positive charge, and high encapsulation efficiency of gene. shBcl-2 loaded in nanoparticles (NPs) was protected effectively from the degradation of DNase I and serum.More importantly, it significantly improved the efficiency of transfection of shRNA in vitro in A549 cells and increased its cytotoxicity and induced more cell apoptosis by silencing Bcl-2.

View Article: PubMed Central - PubMed

Affiliation: School of Pharmacy, Liaoning Medical University, Jinzhou, 121000 People's Republic of China.

ABSTRACT
Protamine nanoparticles were designed by encapsulating small hairpin RNA (shRNA)-expressing plasmid DNA targeting the Bcl-2 gene (shBcl-2) to silence apoptosis-related Bcl-2 protein for improving the transfection efficiency and cytotoxicity in cancer therapy. Our findings demonstrated that the obtained protamine nanoparticles possessed excellent characterizations of small particle size, homogenous distribution, positive charge, and high encapsulation efficiency of gene. shBcl-2 loaded in nanoparticles (NPs) was protected effectively from the degradation of DNase I and serum. More importantly, it significantly improved the efficiency of transfection of shRNA in vitro in A549 cells and increased its cytotoxicity and induced more cell apoptosis by silencing Bcl-2.

No MeSH data available.


Related in: MedlinePlus

Combining ability and protecting effects of shBcl-2-loaded NPs by agarose gel electrophoresis. Gel retardation assay for determining loading ability of shBcl-2 in NPs (A), DNaseI protection of shBcl-2-loaded NPs (B), and serum protection of shBcl-2-loaded NPs (C). (Lane 1: naked shBcl-2; lanes 2 to 4, shBcl-2-loaded NPs prepared at mass ratios of 50,100, and 200, respectively).
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Fig2: Combining ability and protecting effects of shBcl-2-loaded NPs by agarose gel electrophoresis. Gel retardation assay for determining loading ability of shBcl-2 in NPs (A), DNaseI protection of shBcl-2-loaded NPs (B), and serum protection of shBcl-2-loaded NPs (C). (Lane 1: naked shBcl-2; lanes 2 to 4, shBcl-2-loaded NPs prepared at mass ratios of 50,100, and 200, respectively).

Mentions: Positive-charged NPs can encapsulate negative-charged shRNA owing to the strong electrostatic attraction. With the increase of amount of shRNA in NPs, the electrophoretic mobility of DNA is faster and the band will be stronger. The results in FigureĀ 2 showed that when the ratio of protamine and DNA was 100:1, the binding ability of shRNA with NPs was the strongest among the three groups, suggesting that more shRNA was entrapped in NPs.Figure 2


Protamine nanoparticles for improving shRNA-mediated anti-cancer effects.

Liu M, Feng B, Shi Y, Su C, Song H, Cheng W, Zhao L - Nanoscale Res Lett (2015)

Combining ability and protecting effects of shBcl-2-loaded NPs by agarose gel electrophoresis. Gel retardation assay for determining loading ability of shBcl-2 in NPs (A), DNaseI protection of shBcl-2-loaded NPs (B), and serum protection of shBcl-2-loaded NPs (C). (Lane 1: naked shBcl-2; lanes 2 to 4, shBcl-2-loaded NPs prepared at mass ratios of 50,100, and 200, respectively).
© Copyright Policy - open-access
Related In: Results  -  Collection

License
Show All Figures
getmorefigures.php?uid=PMC4385308&req=5

Fig2: Combining ability and protecting effects of shBcl-2-loaded NPs by agarose gel electrophoresis. Gel retardation assay for determining loading ability of shBcl-2 in NPs (A), DNaseI protection of shBcl-2-loaded NPs (B), and serum protection of shBcl-2-loaded NPs (C). (Lane 1: naked shBcl-2; lanes 2 to 4, shBcl-2-loaded NPs prepared at mass ratios of 50,100, and 200, respectively).
Mentions: Positive-charged NPs can encapsulate negative-charged shRNA owing to the strong electrostatic attraction. With the increase of amount of shRNA in NPs, the electrophoretic mobility of DNA is faster and the band will be stronger. The results in FigureĀ 2 showed that when the ratio of protamine and DNA was 100:1, the binding ability of shRNA with NPs was the strongest among the three groups, suggesting that more shRNA was entrapped in NPs.Figure 2

Bottom Line: Protamine nanoparticles were designed by encapsulating small hairpin RNA (shRNA)-expressing plasmid DNA targeting the Bcl-2 gene (shBcl-2) to silence apoptosis-related Bcl-2 protein for improving the transfection efficiency and cytotoxicity in cancer therapy.Our findings demonstrated that the obtained protamine nanoparticles possessed excellent characterizations of small particle size, homogenous distribution, positive charge, and high encapsulation efficiency of gene. shBcl-2 loaded in nanoparticles (NPs) was protected effectively from the degradation of DNase I and serum.More importantly, it significantly improved the efficiency of transfection of shRNA in vitro in A549 cells and increased its cytotoxicity and induced more cell apoptosis by silencing Bcl-2.

View Article: PubMed Central - PubMed

Affiliation: School of Pharmacy, Liaoning Medical University, Jinzhou, 121000 People's Republic of China.

ABSTRACT
Protamine nanoparticles were designed by encapsulating small hairpin RNA (shRNA)-expressing plasmid DNA targeting the Bcl-2 gene (shBcl-2) to silence apoptosis-related Bcl-2 protein for improving the transfection efficiency and cytotoxicity in cancer therapy. Our findings demonstrated that the obtained protamine nanoparticles possessed excellent characterizations of small particle size, homogenous distribution, positive charge, and high encapsulation efficiency of gene. shBcl-2 loaded in nanoparticles (NPs) was protected effectively from the degradation of DNase I and serum. More importantly, it significantly improved the efficiency of transfection of shRNA in vitro in A549 cells and increased its cytotoxicity and induced more cell apoptosis by silencing Bcl-2.

No MeSH data available.


Related in: MedlinePlus