Limits...
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.

Show MeSH
Schematic drawing of the Lys, Mb, and BSA molecules. Trp residues are marked in red.
© Copyright Policy - open-access
Related In: Results  -  Collection

License
getmorefigures.php?uid=PMC3116464&req=5

Figure 1: Schematic drawing of the Lys, Mb, and BSA molecules. Trp residues are marked in red.

Mentions: The present study proposes a novel method for designing a small bioactive nanoparticle using BSA as a carrier to deliver hydrophobic drugs. Quercetin (Q), a polyphenol widely distributed in vegetables and plants, is used here as a model of hydrophobic drugs. Q exhibits anti-oxidative, free radical scavenging, anticancer, and antiviral activities [12]. However, the poor solubility and low stability of Q in aqueous alkaline medium [13] restrict the application of this type of drug in oral use. Dimethyl sulfoxide (DMSO), one of the most versatile organic solvents in biological science that can accept hydrogen-bond and interact with the hydrophobic residues of proteins [14], is used here to dissolve Q, and synthesize a novel nanocarrier with interesting drug delivery capabilities. Some studies have reported that BSA interacts with Q through tryptophan (Trp) [15,16]. BSA is a monomeric globular protein formed from 583 amino acid residues, containing two Trps, one of which is located in the inner hydrophobic pocket, corresponding to the so-called site II. Site II is a specific site for hydrophobic drugs due to its hydrophobicity [11,17]. To confirm the feasibility of the Trp transport functionality, lysozyme (Lys) and myoglobin (Mb) were also used in this work for comparison with BSA. Figure 1 exhibits the molecular structures of Lys, Mb, and BSA. Lys is a small monomeric globular protein formed from 129 amino acid residues, and contains six Trps. This protein is known to bind various small ligands, such as metal ions, non-metal ions, dyes, and numerous pharmaceuticals [18-20]. Mb is a small heme protein for oxygen storage and transport. It contains a single polypeptide chain of 153 amino acid residues and two Trps. The polypeptide chain provides a nonpolar pocket to accommodate and stabilize the porphyrin ring [21-23].


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)

Schematic drawing of the Lys, Mb, and BSA molecules. Trp residues are marked in red.
© Copyright Policy - open-access
Related In: Results  -  Collection

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

Figure 1: Schematic drawing of the Lys, Mb, and BSA molecules. Trp residues are marked in red.
Mentions: The present study proposes a novel method for designing a small bioactive nanoparticle using BSA as a carrier to deliver hydrophobic drugs. Quercetin (Q), a polyphenol widely distributed in vegetables and plants, is used here as a model of hydrophobic drugs. Q exhibits anti-oxidative, free radical scavenging, anticancer, and antiviral activities [12]. However, the poor solubility and low stability of Q in aqueous alkaline medium [13] restrict the application of this type of drug in oral use. Dimethyl sulfoxide (DMSO), one of the most versatile organic solvents in biological science that can accept hydrogen-bond and interact with the hydrophobic residues of proteins [14], is used here to dissolve Q, and synthesize a novel nanocarrier with interesting drug delivery capabilities. Some studies have reported that BSA interacts with Q through tryptophan (Trp) [15,16]. BSA is a monomeric globular protein formed from 583 amino acid residues, containing two Trps, one of which is located in the inner hydrophobic pocket, corresponding to the so-called site II. Site II is a specific site for hydrophobic drugs due to its hydrophobicity [11,17]. To confirm the feasibility of the Trp transport functionality, lysozyme (Lys) and myoglobin (Mb) were also used in this work for comparison with BSA. Figure 1 exhibits the molecular structures of Lys, Mb, and BSA. Lys is a small monomeric globular protein formed from 129 amino acid residues, and contains six Trps. This protein is known to bind various small ligands, such as metal ions, non-metal ions, dyes, and numerous pharmaceuticals [18-20]. Mb is a small heme protein for oxygen storage and transport. It contains a single polypeptide chain of 153 amino acid residues and two Trps. The polypeptide chain provides a nonpolar pocket to accommodate and stabilize the porphyrin ring [21-23].

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