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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 DMSO. The concentration of Lys was 1.5 × 10-5 mol/L. (a) Native Lys; (b) Lys and 10% DMSO; (c) Lys and 30% DMSO; (d) Lys and 50% DMSO; (e) Lys and 70% DMSO.
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Figure 8: Raman spectrum of Lys system vs. the concentration of DMSO. The concentration of Lys was 1.5 × 10-5 mol/L. (a) Native Lys; (b) Lys and 10% DMSO; (c) Lys and 30% DMSO; (d) Lys and 50% DMSO; (e) Lys and 70% DMSO.

Mentions: Raman spectroscopy was employed to investigate changes in the secondary and tertiary structures of the protein molecules during aggregation. Figure 7 compares the Raman spectra of native BSA and D-BSA in the 1800-400 cm-1 region. Consistent with the literature [26,27], the secondary structure of native BSA was largely α-helical in form; this was supported by an amide I signal at 1654 cm-1. The decrease in band intensity with DMSO concentration presented in Table 1 indicates the loss of the α-helix during aggregation. Meanwhile, the broadening of this band and the increase of the band intensity at 1665 cm-1 implies the increase of the random-coil content in the protein structure [26].The coincident trends were observed in Lys (Figure 8) and Mb (Figure 9) systems. Over 30% of the secondary structure of native Lys presented in random coil conformation, as supported by an amide I signal at 1665 cm-1 and an amide III signal at 1245 cm-1. The change in intensity of these bands, presented in Table 2, shows the increase of random-coil in protein microstructures with DMSO. The secondary structure of the native Mb was largely α-helical in form, as supported by an amide I signal at 1659 cm-1. Similar to the case of D-BSA, the disappearance of this band with DMSO concentration, presented in Table 3, indicates the decrease of α-helix during aggregation. The increase in intensity of the band at 1669 cm-1 implies an increase in random-coil content in the protein structure during aggregation. The loss of the α-helix is attributed to the competition between the S = O group of DMSO and the C = O groups of protein for the amide's hydrogen molecules, resulting in the partial unfolding of the polypeptide chain, exposure of the internal hydrophobic groups, and promotion of protein aggregation by hydrophobic effects and H-bonding [14,28]. This belief is supported by the zeta potential measurements in the previous section.


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 DMSO. The concentration of Lys was 1.5 × 10-5 mol/L. (a) Native Lys; (b) Lys and 10% DMSO; (c) Lys and 30% DMSO; (d) Lys and 50% DMSO; (e) Lys and 70% DMSO.
© Copyright Policy - open-access
Related In: Results  -  Collection

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Figure 8: Raman spectrum of Lys system vs. the concentration of DMSO. The concentration of Lys was 1.5 × 10-5 mol/L. (a) Native Lys; (b) Lys and 10% DMSO; (c) Lys and 30% DMSO; (d) Lys and 50% DMSO; (e) Lys and 70% DMSO.
Mentions: Raman spectroscopy was employed to investigate changes in the secondary and tertiary structures of the protein molecules during aggregation. Figure 7 compares the Raman spectra of native BSA and D-BSA in the 1800-400 cm-1 region. Consistent with the literature [26,27], the secondary structure of native BSA was largely α-helical in form; this was supported by an amide I signal at 1654 cm-1. The decrease in band intensity with DMSO concentration presented in Table 1 indicates the loss of the α-helix during aggregation. Meanwhile, the broadening of this band and the increase of the band intensity at 1665 cm-1 implies the increase of the random-coil content in the protein structure [26].The coincident trends were observed in Lys (Figure 8) and Mb (Figure 9) systems. Over 30% of the secondary structure of native Lys presented in random coil conformation, as supported by an amide I signal at 1665 cm-1 and an amide III signal at 1245 cm-1. The change in intensity of these bands, presented in Table 2, shows the increase of random-coil in protein microstructures with DMSO. The secondary structure of the native Mb was largely α-helical in form, as supported by an amide I signal at 1659 cm-1. Similar to the case of D-BSA, the disappearance of this band with DMSO concentration, presented in Table 3, indicates the decrease of α-helix during aggregation. The increase in intensity of the band at 1669 cm-1 implies an increase in random-coil content in the protein structure during aggregation. The loss of the α-helix is attributed to the competition between the S = O group of DMSO and the C = O groups of protein for the amide's hydrogen molecules, resulting in the partial unfolding of the polypeptide chain, exposure of the internal hydrophobic groups, and promotion of protein aggregation by hydrophobic effects and H-bonding [14,28]. This belief is supported by the zeta potential measurements in the previous section.

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