Inhomogeneity in Distribution and Conformation of Bovine Serum Albumin in Sol?Gel: A Closer Look with a Near-Infrared Multispectral Imaging Technique

Tran, Chieu D.; Ilieva, D.; Challa, Santhosh

doi:10.1007/s10971-004-5790-8

Cited by 7 publications

(4 citation statements)

References 21 publications

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“…It is not affected by various detergents and denaturing agents, such as urea and guanidinium chloride, although it is more sensitive to the 13 presence of reducing sugars. The calibration curve was prepared over a sample concentration range from 0.4 μg/ mL to 20 μg/mL.…”

Section: Bca Microassaymentioning

confidence: 99%

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Preparation and Release Properties of Sol-Gel Encapsulated Proteins

Chen¹,

Liu²,

Yang³

et al. 2013

JASMI

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A glycoprotein, bovine serum albumin (BSA) was used as a model compound for encapsulation in a sol-gel matrix. Dried gels were ground into powders and meshed to achieve particle sizes less than 250 μm. The products were washed with phosphate buffer. Capillary electrophoresis was used to evaluate the encapsulation efficiency and the kinetic properties of protein release. Several parameters, including the pH and composition of the background electrolyte, were investigated in an effort to eliminate the matrix effect from the determination of release kinetics. Complete separation of the silica matrix from BSA was using phosphate buffer, an applied voltage of 15 kV, and detection at 278 nm. Kinetic studies indicated that most of the BSA was released in the first 5 h. The rate of BSA release gradually decreased, and some BSA after 25 h. These results indicated that dilute potassium phosphate buffer could accelerate protein release, but this was not observed for the concentrations greater than 50 mM. We believe the developed method has potential utility in other systems for in vitro matrix dissolution and drug release studies.

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Section: Bca Microassaymentioning

confidence: 99%

“…BSA is a well-studied biomolecule among the wide variety of biological species that have been encapsulated in sol-gel matrices [11][12][13]. Gao et al [14] have studied the structural evolution of sol-gel matrices in the presence of BSA.…”

Section: Introductionmentioning

confidence: 99%

Preparation and Release Properties of Sol-Gel Encapsulated Proteins

Chen¹,

Liu²,

Yang³

et al. 2013

JASMI

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“…Among the wide variety of biological species that have been encapsulated in sol−gel matrices, bovine serum albumin (BSA) is a well-studied biomolecule that has been immobilized in the silica matrix via the sol−gel processing. − It has a single chain with 582 amino acid residues folded into three globular domains. Zhang et al studied the protein interaction using SAXS and reported the dimensions of 1.7 × 4.2 × 4.2 nm from their simulations using an oblate ellipsoid form factor.…”

Section: Introductionmentioning

confidence: 99%

“…The isoelectric point of BSA is at pH 4.7, and hence at neutral pH BSA carries a net negative charge . Tran et al have encapsulated the BSA in silica via the sol−gel process using tetramethyoxysilane (TMOS) as precursor. They reported that regardless of the BSA concentration the protein was inhomogeneously distributed within the sol−gel matrix due to interactions between the silicate anions and the negatively charged protein.…”

Section: Introductionmentioning

confidence: 99%

Encapsulation of Protein in Silica Matrices: Structural Evolution on the Molecular and Nanoscales

et al. 2009

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The immobilization of biological species such as proteins and enzymes in sol-gel hosts is currently an area of intense research activity. However, the majority of these studies have been directed toward investigating the biological activity or physicochemical properties of the encapsulated species, with much less attention having been directed toward the effect of proteins on the structural evolution of the sol-gel matrix. This study investigates the structural evolution of sol-gel matrices in the presence of a model protein, bovine serum albumin (BSA). The sol-gel matrices were produced via the NaF-catalyzed hydrolysis of a mixture of tetramethyoxysilane (TMOS) and methyltrimethoxysilane (MTMS), yielding nanohybrid matrices with controlled pore sizes, pore volumes, and surface chemistry. The structural evolution of the matrix was investigated using a complementary suite of techniques, including solid-state (29)Si NMR, FTIR, SANS contrast variation, and N(2) sorption. A novel approach was developed to model the SANS data, to extract key structural parameters. The results indicated that the structural evolution of the matrices was modulated by a series of complex interactions between the enzyme and the evolving sol-gel nanohybrid: On the molecular scale, increasing BSA content led to an associated increase in both the abundance of linear Si-O-Si species (FTIR) and the Qn network connectivity ((29)Si NMR). However, only minor changes in the connectivity of the evolving Tn network were evident with varying BSA content. The selective role of the protein in these systems, where the approach of the methylated monomer to the vicinity of the protein's surface is presumably impeded by the hydrophobicity of the monomer, will be discussed. On the nanoscale, N(2) sorption data were consistent with an initial increase in the mesopore volume and surface area at low BSA loadings, followed by a subsequent monotonic decrease with increasing BSA content. In contrast, no such trends were evident in the in situ SANS data obtained from these samples, suggesting that modulation of the evolving network structure of the silica matrix by BSA during condensation prevents collapse of the nanoscale gel structure during freeze-drying. This latter comparison reflects the important role of in situ techniques such as small angle scattering (which can be used to study both open and closed porosity and probe nanostructure on length scales from approximately 1 nm to>100 nm) in investigating such complex, multicomponent systems, and techniques for modeling such data in sol-gel systems will be discussed.

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