Biopolymer albumin for diagnosis and in drug delivery

Patil, Gayathri V.

doi:10.1002/ddr.10157

Cited by 152 publications

(93 citation statements)

References 166 publications

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“…Computer simulations show that eq 9 is reasonably accurate even for very dense hard-sphere fluids. 37 We comment that, when φ is small, the overlapping of the depletion layers can be neglected and eq 9 becomes R ≈ 1 -(1 + q) 3 φ. This is true even when R (1) and higher-order terms are included.…”

Section: Discussionmentioning

confidence: 97%

“…1,2 In pharmaceutical science, it is important for the preparation of protein microspheres relevant to drug delivery. 3,4 In enzymology, it is important for the preparation of novel cross-linked enzyme particles for catalysis in aqueous and nonaqueous media. 5,6 However, a sound scientific basis of the thermodynamic behavior of protein aqueous solutions is still missing.…”

Section: Introductionmentioning

confidence: 99%

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Comparison between Protein−Polyethylene Glycol (PEG) Interactions and the Effect of PEG on Protein−Protein Interactions Using the Liquid−Liquid Phase Transition

Wang

Annunziata

2007

J. Phys. Chem. B

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Phase transitions of protein aqueous solutions are important for protein crystallization and biomaterials science in general. One source of thermodynamic complexity in protein solutions and their phase transitions is the required presence of additives such as polyethylene glycol (PEG). To investigate the effects of PEG on the thermodynamic behavior of protein solutions, we report measurements on the liquid-liquid phase separation (LLPS) of aqueous bovine serum albumin (BSA) in the presence of relatively small amounts of PEG with an average molecular weight of 1450 g/mol (PEG1450) as a model system. We experimentally characterize two thermodynamically independent properties of the phase boundary: (1) the effect of PEG1450 concentration on the LLPS temperature, (2) BSA/PEG1450 partitioning in the two liquid coexisting phases. We then use a thermodynamic perturbation theory to relate the first property to the effect of PEG concentration on proteinprotein interactions and the second property to protein-PEG interactions. As criteria to determine the accuracy of a microscopic model, we examine the model's ability to describe both experimental thermodynamic properties. We believe that the parallel examination of these two properties is a valuable tool for verifying the validity of existing models and for developing more accurate ones. For our system, we have found that a depletion-interaction model satisfactorily explains both protein-PEG interactions and the effect of PEG concentration on protein-protein interactions. Finally, due to the general importance of LLPS, we will experimentally show that protein-PEG-buffer mixtures can exhibit two distinct types of liquid-liquid phase transitions.

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Section: Discussionmentioning

confidence: 97%

Section: Introductionmentioning

confidence: 99%

Comparison between Protein−Polyethylene Glycol (PEG) Interactions and the Effect of PEG on Protein−Protein Interactions Using the Liquid−Liquid Phase Transition

Wang

Annunziata

2007

J. Phys. Chem. B

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“…Their small size permits them to be injected intravenously to reach target tissues. Among them, nanoparticulate systems based on proteins have gained much interest because of their inherent properties of biodegradability, lack of toxicity, and nonantigenicity (1,2). Protein nanoparticles may be used as a matrix in which a wide variety of drugs can be physically entrapped (3)(4)(5).…”

Section: Introductionmentioning

confidence: 99%

Optimization of PEGylation Conditions for BSA Nanoparticles Using Response Surface Methodology

et al. 2010

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Abstract. Chemical coupling of polyethylene glycol (PEG) to proteins or particles (PEGylation), prolongs their circulation half-life by greater than 50-fold, reduces their immunogenicity, and also promotes their accumulation in tumors due to enhanced permeability and retention effect. Herein, phase separation method was used to prepare bovine serum albumin (BSA) nanoparticles. PEGylation of BSA nanoparticles was performed by SPA activated mPEG through their free amino groups. Effect of process variables on PEGylation efficiency of BSA nanoparticles was investigated and optimized through response surface methodology with the amount of free amino groups as response. Optimum conditions was found to be 32.5 g/l of PEG concentration, PEG-nanoparticle incubation time of 10 min, incubation temperature of 27°C, and pH of 7 for 5 mg of BSA nanoparticles in 1 mL phosphate buffer. Analysis of data showed that PEG concentration had the most noticeable effect on the amount of PEGylated amino groups, but pH had the least. Mean diameter and zeta potential of PEGylated nanoparticles under these conditions were 217 nm and −14 mV, respectively. In conclusion, PEGylated nanoparticles demonstrated reduction of the negative surface charge compared to the non modified particles with the zeta potential of −31.7 mV. Drug release from PEGylated nanoparticles was almost slower than non-PEGylated ones, probably due to existence of a PEG layer around PEGylated particles which makes an extra resistance in opposition to drug diffusion.

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“…They may be built up from either synthetic or natural macromolecules. Natural macromolecules, and above all proteins, have gained much interest as biomaterials owing to their inherent properties of biodegradability, lack of toxicity, and nonantigenicity (1)(2)(3)(4). Colloidal systems based on proteins might be incredibly promising as they unite the advantages of nanoparticles with the advantages of covalent protein-drug conjugates (5,6).…”

Section: Introductionmentioning

confidence: 99%

5-Fluorouracil-Loaded BSA Nanoparticles: Formulation Optimization and In Vitro Release Study

2008

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Abstract. Over the past few decades, there has been considerable interest in developing protein nanoparticles as drug delivery devices. The underlying rationale is their exceptional characteristics, namely biodegradability and nonantigenicity. Herein, phase separation method was used to prepare 5-fluorouracil-loaded bovine serum albumin (BSA) nanoparticles. Drug release was tracked by continuous flow dialysis technique. Effect of process variables on loading efficiency of 5-fluorouracil was investigated and optimized through Taguchi's M16 design with the amount of entrapped drug as response. Optimum condition was found to be 2 mg/mL of 5-fluorouracil, 3.7 mL of added ethanol, 176 µL of glutaraldehyde, drug-protein incubation time of 30 min, and pH of 8.4 for 200 mg of BSA in 2 mL drug solution. pH had the most noticeable effect on the amount of entrapped drug, but glutaraldehyde had the least. Mean diameter and zeta potential of fabricated nanoparticles under these conditions were 210 nm and −31.7 mV, respectively. Drug-loaded BSA nanoparticles suspension maintained constant release of drug for 20 h under experimental conditions, so this colloidal drug carrier is capable of releasing drug in a sustained manner.

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Biopolymer albumin for diagnosis and in drug delivery

Cited by 152 publications

References 166 publications

Comparison between Protein−Polyethylene Glycol (PEG) Interactions and the Effect of PEG on Protein−Protein Interactions Using the Liquid−Liquid Phase Transition

Comparison between Protein−Polyethylene Glycol (PEG) Interactions and the Effect of PEG on Protein−Protein Interactions Using the Liquid−Liquid Phase Transition

Optimization of PEGylation Conditions for BSA Nanoparticles Using Response Surface Methodology

5-Fluorouracil-Loaded BSA Nanoparticles: Formulation Optimization and In Vitro Release Study

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