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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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Raman spectrum of Lys system vs. the concentration of Q. The concentrations of Lys and DMSO were maintained at 1.5 × 10-5 mol/L and 10%, respectively. (a) 0 mol/L Q; (b) 3.0 × 10-5 mol/L Q; (c) 9.0 × 10-5 mol/L Q; (d) 1.5 × 10-4 mol/L Q.
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Figure 11: Raman spectrum of Lys system vs. the concentration of Q. The concentrations of Lys and DMSO were maintained at 1.5 × 10-5 mol/L and 10%, respectively. (a) 0 mol/L Q; (b) 3.0 × 10-5 mol/L Q; (c) 9.0 × 10-5 mol/L Q; (d) 1.5 × 10-4 mol/L Q.

Mentions: The Raman spectra of D-BSA-Q and D-Lys-Q are shown in Figures 10 and 11, respectively; here, the concentration of DMSO was kept constant at 10%. The band at 1611 cm-1 (Figures 10 and 11), which is sensitive to the bound ligands, is a marker of the orientation of the indole ring of Trp with respect to the Cα atom of the peptide backbone [29]. The increase in band intensities shown in Tables 4 and 5 indicates that the added Q led to the reorientation of the indole ring through the adjustment in the torsional angle of the side chain. The bands near 1319 and 600 cm-1 were ascribed to aliphatic CH2 twisting deformations and the pyrrole ring skeletal of Trp [30], respectively. The significant increase in their intensities with increasing Q proved the interactions between Trp and Q (Figures 10 and 11, Tables 4 and 5). The bands near 1339 [31,32] and 758 [33] cm-1 have been found to be indicators of the hydrophobicity of the Trp environment, and a decrease in these band intensities (Figures 10 and 11, Tables 4 and 5) indicates that the molecular environment of Trp is more hydrophobic due to the interactions between the indole ring and Q.


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)

Raman spectrum of Lys system vs. the concentration of Q. The concentrations of Lys and DMSO were maintained at 1.5 × 10-5 mol/L and 10%, respectively. (a) 0 mol/L Q; (b) 3.0 × 10-5 mol/L Q; (c) 9.0 × 10-5 mol/L Q; (d) 1.5 × 10-4 mol/L Q.
© Copyright Policy - open-access
Related In: Results  -  Collection

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

Figure 11: Raman spectrum of Lys system vs. the concentration of Q. The concentrations of Lys and DMSO were maintained at 1.5 × 10-5 mol/L and 10%, respectively. (a) 0 mol/L Q; (b) 3.0 × 10-5 mol/L Q; (c) 9.0 × 10-5 mol/L Q; (d) 1.5 × 10-4 mol/L Q.
Mentions: The Raman spectra of D-BSA-Q and D-Lys-Q are shown in Figures 10 and 11, respectively; here, the concentration of DMSO was kept constant at 10%. The band at 1611 cm-1 (Figures 10 and 11), which is sensitive to the bound ligands, is a marker of the orientation of the indole ring of Trp with respect to the Cα atom of the peptide backbone [29]. The increase in band intensities shown in Tables 4 and 5 indicates that the added Q led to the reorientation of the indole ring through the adjustment in the torsional angle of the side chain. The bands near 1319 and 600 cm-1 were ascribed to aliphatic CH2 twisting deformations and the pyrrole ring skeletal of Trp [30], respectively. The significant increase in their intensities with increasing Q proved the interactions between Trp and Q (Figures 10 and 11, Tables 4 and 5). The bands near 1339 [31,32] and 758 [33] cm-1 have been found to be indicators of the hydrophobicity of the Trp environment, and a decrease in these band intensities (Figures 10 and 11, Tables 4 and 5) indicates that the molecular environment of Trp is more hydrophobic due to the interactions between the indole ring and Q.

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