Studies on Thermal Aggregation of Bovine Serum Albumin as a Drug Carrier.

Honda, Chikako; Kamizono, Hiroko; Samejima, Tomomi; Endo, Kazutoyo

doi:10.1248/cpb.48.464

Cited by 32 publications

(16 citation statements)

References 1 publication

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“…Bovine serum albumin (BSA) has been extensively used as a model to study protein aggregation [6,8,24,27,34,35,48,49,51] and fibrillation [10,48]. BSA is essentially an all a protein, which is transformed to b-form upon destabilizing conditions [23,24,36].…”

Section: Introductionmentioning

confidence: 99%

Response Surface Methodology for Optimizing the Bovine Serum Albumin Fibrillation

et al. 2012

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Amyloid fibrils are considered as nanostructures that could be formed by ordered self-assembly of the partially-folded states of many different peptides or proteins. In this study, bovine serum albumin was used as a model protein whose ordered aggregation (fibrillation) was optimized. Response surface methodology (RSM) was used in a design that contained a total of 30 experimental trials. The first 24 were organized in a factorial design and from 25 to 30 involved the replications of the central points. Data obtained from RSM were subjected to the analysis of variance (ANOVA) and analyzed using a second order polynomial equation. Subsequent testing of the suggested experimental parameters was done in vitro with Congo red spectrophotometric assay. Protein concentration, pH, temperature and time of incubation were the variables used in this study. Responses were assessed by measuring absorbance in 540 nm (characteristic of amyloid formation) and maximal wavelength. Concomitant effects of variables were assessed in surface plots that each considered two of the variables. Interestingly, the pattern obtained by monitoring absorbance at 540 nm and absorbance in maximal wavelength were identical in most cases. We are reporting the optimum concentration of protein, pH, temperature and time at 5 mg ml⁻¹, 3.02 and 72 °C and 48 h, respectively. Our findings suggest that use of Congo red spectrophotometric test, as a simple and affordable assay could be suggested as a first test for assessing fibril formation of proteins. Absorbance in maximal wavelength is recommended as a significant indication of fibril formation.

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Section: Introductionmentioning

confidence: 99%

Response Surface Methodology for Optimizing the Bovine Serum Albumin Fibrillation

et al. 2012

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“…Similarly, treatment of proteins with stress conditions (heat, chemical denaturants) is accompanied by aggregation of denatured protein molecules (Joly, 1965;Lohner and Esser, 1991;Honda et al, 2000;Villaverde and Carrio, 2003;Weijers et al, 2003).…”

Section: Introductionmentioning

confidence: 99%

Prevention of thermal induced aggregation of cytochrome c at isoelectric pH values by polyanions

Fedunova

Antalı́k

2006

Biotech & Bioengineering

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Differential scanning calorimetry, viscometry, optical and CD spectroscopy were used to characterize the influence of two polyanions, poly(vinylsulfate) (PVS), and poly(4-styrene-sulfonate) (PSS) on thermal transition reversibility of ferricytochrome c at or near isoelectric pH. In these conditions, both PVS and PSS enhance the thermal transition reversibility of cytochrome c by preventing the aggregation of denatured protein molecules. Data indicate that the polyanions are in complex with cytochrome c that is stabilized by synergistic effect of Coulombic and non-Coulombic interactions.

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“…31 At the secondary structure level, there is a partial loose of the a-helix and an increase in antiparallel b-sheet attributing to the formation of non-native b-sheet associated with aggregation. 30,32,[36][37][38] At a molecular level, the number of hydrogen bonds increases aer gelation and it increases with the increase of BSA concentration. This claim is clearly supported by the increased intensity in 3000-3600 cm À1 region, which attributes to increasing N-H groups in appearance of carboxyl groups.…”

Section: Bsa Hydrogelmentioning

confidence: 99%

Self-healing of thermally-induced, biocompatible and biodegradable protein hydrogel

Dong

Song

et al. 2016

RSC Adv.

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Serum albumin is the most abundant protein in the circulatory system to transport fatty acids, metabolites and drugs. In this study, a highly biocompatible protein hydrogel was prepared from bovine serum albumin (BSA) via thermal treatment. A circular dichroism study indicates that thermally-induced partial unfolding of the protein molecules exposes the buried hydrophobic groups in the core to the environment, thus leading to the formation of fine stranded 3-D networks. By controlling the heating temperature and protein concentration, the mechanical strength and structural stability of the as-prepared BSA hydrogel can be facilely manipulated. The moderate denaturation of the protein within the hydrogel system allows repetitive self-healing after damage when moderate heat was induced. The tensile strength and break strain of fully healed protein hydrogel were recovered to almost 100% of the original strength and elongation abilities. Additionally, the good biocompatibility of this hydrogel system was demonstrated through in vitro cytotoxicity analysis first. Furthermore, in vivo experiments using immunocompetent mice show that the subcutaneously injected hydrogel in mice can be fully degraded with negligible acute inflammatory response, indicating excellent in vivo biocompatibility. These features indicate that the as-developed self-healing protein hydrogel system with good biocompatibility and biodegradability holds great potential in the field of biomedical engineering.

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Studies on Thermal Aggregation of Bovine Serum Albumin as a Drug Carrier.

Cited by 32 publications

References 1 publication

Response Surface Methodology for Optimizing the Bovine Serum Albumin Fibrillation

Response Surface Methodology for Optimizing the Bovine Serum Albumin Fibrillation

Prevention of thermal induced aggregation of cytochrome c at isoelectric pH values by polyanions

Self-healing of thermally-induced, biocompatible and biodegradable protein hydrogel

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