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Design and characterization of protein-quercetin bioactive nanoparticles.

Fang R, Jing H, Chai Z, Zhao G, Stoll S, Ren F, Liu F, Leng X - J Nanobiotechnology (2011)

Bottom Line: After loading Q, the size was further reduced by 30%.The controlled releasing measurements indicate that these bioactive nanoparticles have long-term antioxidant protection effects on the activity of Q in both acidic and neutral conditions.BSA exhibits the most remarkable abilities of loading, controlled release, and antioxidant protection of active drugs, indicating that such type of bionanoparticles is very promising in the field of bionanotechnology.

View Article: PubMed Central - HTML - PubMed

Affiliation: CAU and ACC Joint Laboratory of Space Food, College of Food Science and Nutritional Engineering, China Agricultural University, Beijing 100083, China.

ABSTRACT

Background: The synthesis of bioactive nanoparticles with precise molecular level control is a major challenge in bionanotechnology. Understanding the nature of the interactions between the active components and transport biomaterials is thus essential for the rational formulation of bio-nanocarriers. The current study presents a single molecule of bovine serum albumin (BSA), lysozyme (Lys), or myoglobin (Mb) used to load hydrophobic drugs such as quercetin (Q) and other flavonoids.

Results: Induced by dimethyl sulfoxide (DMSO), BSA, Lys, and Mb formed spherical nanocarriers with sizes less than 70 nm. After loading Q, the size was further reduced by 30%. The adsorption of Q on protein is mainly hydrophobic, and is related to the synergy of Trp residues with the molecular environment of the proteins. Seven Q molecules could be entrapped by one Lys molecule, 9 by one Mb, and 11 by one BSA. The controlled releasing measurements indicate that these bioactive nanoparticles have long-term antioxidant protection effects on the activity of Q in both acidic and neutral conditions. The antioxidant activity evaluation indicates that the activity of Q is not hindered by the formation of protein nanoparticles. Other flavonoids, such as kaempferol and rutin, were also investigated.

Conclusions: BSA exhibits the most remarkable abilities of loading, controlled release, and antioxidant protection of active drugs, indicating that such type of bionanoparticles is very promising in the field of bionanotechnology.

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Comparison of the quantity of the oxidized Q in the system without or with protein. The concentrations of Q and protein (BSA, Lys, and Mb) were 1.5 × 10-4 and 1.5 × 10-5 mol/L, respectively. Q solution was prepared with 10% DMSO. (A) Measurements during 216 hours. (B) Measurements during the first 24 hours at pH 7.4. Black square refers to Q without protein at pH 1.2; balck rhombus refers to Q with BSA at pH 1.2; black upper triangle refers to Q with Lys at pH 1.2; black lower triangle refers to Q with Mb at pH 1.2; white square refers to Q without protein at pH 7.4; white rhombus refers to Q with BSA at pH 7.4; white upper triangle refers to Q with Lys at pH 7.4; white lower triangle refers to Q with Mb at pH 7.4.
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Figure 17: Comparison of the quantity of the oxidized Q in the system without or with protein. The concentrations of Q and protein (BSA, Lys, and Mb) were 1.5 × 10-4 and 1.5 × 10-5 mol/L, respectively. Q solution was prepared with 10% DMSO. (A) Measurements during 216 hours. (B) Measurements during the first 24 hours at pH 7.4. Black square refers to Q without protein at pH 1.2; balck rhombus refers to Q with BSA at pH 1.2; black upper triangle refers to Q with Lys at pH 1.2; black lower triangle refers to Q with Mb at pH 1.2; white square refers to Q without protein at pH 7.4; white rhombus refers to Q with BSA at pH 7.4; white upper triangle refers to Q with Lys at pH 7.4; white lower triangle refers to Q with Mb at pH 7.4.

Mentions: Figure 17 compares the quantity of oxidized Q in the system, without or with proteins, in acidic and neutral conditions (A), and shows the enlarged part of the curves at pH 7.4 during the first 24 h of reaction (B). Q was rapidly auto-oxidized by O2 in water to form o-quinone/quinone methide [13,51-53]. Since only the free Q could be easily oxidized, the curves in Figure 17 are equivalent to the curves of the release capacity of the proteins. Q was relatively stable in acidic conditions, and no oxidation was observed during the first 96 h of the reaction. BSA, Lys, and Mb administration extended the steady state to 120 h. In neutral conditions, Q became very unstable. In Figure 17B, more than 90% of the Q in the system without protein rapidly oxidized during the first 24 h of the reaction. Evidently, the kinetics of oxidation was greatly reduced by the BSA nanocarrier, i.e., less than 10% of the Q was oxidized during the first 24 h of reaction, and less than 70% of the Q was oxidized at 216 h. This protection was not provided by the Lys and Mb nanocarriers.


Design and characterization of protein-quercetin bioactive nanoparticles.

Fang R, Jing H, Chai Z, Zhao G, Stoll S, Ren F, Liu F, Leng X - J Nanobiotechnology (2011)

Comparison of the quantity of the oxidized Q in the system without or with protein. The concentrations of Q and protein (BSA, Lys, and Mb) were 1.5 × 10-4 and 1.5 × 10-5 mol/L, respectively. Q solution was prepared with 10% DMSO. (A) Measurements during 216 hours. (B) Measurements during the first 24 hours at pH 7.4. Black square refers to Q without protein at pH 1.2; balck rhombus refers to Q with BSA at pH 1.2; black upper triangle refers to Q with Lys at pH 1.2; black lower triangle refers to Q with Mb at pH 1.2; white square refers to Q without protein at pH 7.4; white rhombus refers to Q with BSA at pH 7.4; white upper triangle refers to Q with Lys at pH 7.4; white lower triangle refers to Q with Mb at pH 7.4.
© Copyright Policy - open-access
Related In: Results  -  Collection

License
Show All Figures
getmorefigures.php?uid=PMC3116464&req=5

Figure 17: Comparison of the quantity of the oxidized Q in the system without or with protein. The concentrations of Q and protein (BSA, Lys, and Mb) were 1.5 × 10-4 and 1.5 × 10-5 mol/L, respectively. Q solution was prepared with 10% DMSO. (A) Measurements during 216 hours. (B) Measurements during the first 24 hours at pH 7.4. Black square refers to Q without protein at pH 1.2; balck rhombus refers to Q with BSA at pH 1.2; black upper triangle refers to Q with Lys at pH 1.2; black lower triangle refers to Q with Mb at pH 1.2; white square refers to Q without protein at pH 7.4; white rhombus refers to Q with BSA at pH 7.4; white upper triangle refers to Q with Lys at pH 7.4; white lower triangle refers to Q with Mb at pH 7.4.
Mentions: Figure 17 compares the quantity of oxidized Q in the system, without or with proteins, in acidic and neutral conditions (A), and shows the enlarged part of the curves at pH 7.4 during the first 24 h of reaction (B). Q was rapidly auto-oxidized by O2 in water to form o-quinone/quinone methide [13,51-53]. Since only the free Q could be easily oxidized, the curves in Figure 17 are equivalent to the curves of the release capacity of the proteins. Q was relatively stable in acidic conditions, and no oxidation was observed during the first 96 h of the reaction. BSA, Lys, and Mb administration extended the steady state to 120 h. In neutral conditions, Q became very unstable. In Figure 17B, more than 90% of the Q in the system without protein rapidly oxidized during the first 24 h of the reaction. Evidently, the kinetics of oxidation was greatly reduced by the BSA nanocarrier, i.e., less than 10% of the Q was oxidized during the first 24 h of reaction, and less than 70% of the Q was oxidized at 216 h. This protection was not provided by the Lys and Mb nanocarriers.

Bottom Line: After loading Q, the size was further reduced by 30%.The controlled releasing measurements indicate that these bioactive nanoparticles have long-term antioxidant protection effects on the activity of Q in both acidic and neutral conditions.BSA exhibits the most remarkable abilities of loading, controlled release, and antioxidant protection of active drugs, indicating that such type of bionanoparticles is very promising in the field of bionanotechnology.

View Article: PubMed Central - HTML - PubMed

Affiliation: CAU and ACC Joint Laboratory of Space Food, College of Food Science and Nutritional Engineering, China Agricultural University, Beijing 100083, China.

ABSTRACT

Background: The synthesis of bioactive nanoparticles with precise molecular level control is a major challenge in bionanotechnology. Understanding the nature of the interactions between the active components and transport biomaterials is thus essential for the rational formulation of bio-nanocarriers. The current study presents a single molecule of bovine serum albumin (BSA), lysozyme (Lys), or myoglobin (Mb) used to load hydrophobic drugs such as quercetin (Q) and other flavonoids.

Results: Induced by dimethyl sulfoxide (DMSO), BSA, Lys, and Mb formed spherical nanocarriers with sizes less than 70 nm. After loading Q, the size was further reduced by 30%. The adsorption of Q on protein is mainly hydrophobic, and is related to the synergy of Trp residues with the molecular environment of the proteins. Seven Q molecules could be entrapped by one Lys molecule, 9 by one Mb, and 11 by one BSA. The controlled releasing measurements indicate that these bioactive nanoparticles have long-term antioxidant protection effects on the activity of Q in both acidic and neutral conditions. The antioxidant activity evaluation indicates that the activity of Q is not hindered by the formation of protein nanoparticles. Other flavonoids, such as kaempferol and rutin, were also investigated.

Conclusions: BSA exhibits the most remarkable abilities of loading, controlled release, and antioxidant protection of active drugs, indicating that such type of bionanoparticles is very promising in the field of bionanotechnology.

Show MeSH