Protection of Bovine Serum Albumin from Aggregation by Tween 80

Arakawa, Tsutomu; Kita, Yoshiko

doi:10.1002/(sici)1520-6017(200005)89:5<646::aid-jps10>3.0.co;2-j

Cited by 86 publications

(23 citation statements)

References 16 publications

(10 reference statements)

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“…Tween 80 was shown to inhibit thermally induced aggregation of BSA. 229 Poloxamers 407 and 188 (Pluronic F68) were shown to inhibit thermally induced aggregation of rhGH and methionyl pGH. 230 On the other hand, the effects of surfactants on protein aggregation have not been consistent among different proteins.…”

Section: Nonionic Surfactantsmentioning

confidence: 99%

External Factors Affecting Protein Aggregation

Wang

Speaker

2010

Aggregation of Therapeutic Proteins

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The behavior of biotherapeutic proteins is signifi cantly different from small molecule drugs both in liquid and solid states, especially in terms of physical stability. One such property is the high tendency of protein molecules to aggregate under a variety of conditions. The aggregation tendency is arguably the most common and troubling manifestation of protein instability during the development of protein biotherapeutics. 1 Protein aggregates usually exhibit either reduced or, in many cases, no biological activity. 2 -5 A clear correlation was established between loss of recombinant factor VIII (rFVIII ) and its degree of aggregation as shown in Fig. 4.1 . 6 To achieve effective prevention or inhibition of protein aggregation, it is of paramount importance to understand all the possible factors that affect or control the protein aggregation process.Many factors have been identifi ed and reported in the literature affecting the process and rate of protein aggregation. These factors can be roughly divided into two major categories: internal (protein structure related) and external (protein environment related). Chapter 3 in this book has focused extensively on factors that belong to the fi rst category. This chapter focuses on the external factors that affect the process and rate of protein aggregation. To facilitate discussion, these external factors are further divided into the following sections: (1) temperature; (2) solution conditions and composition (pH, buffer type and concentration, ionic strength, excipients and level, protein concentration, metal ions, denaturing and reducing agents, impurities, organic solvents, containers/closures, sources of proteins, sample treatment, and analytical methodologies); (3) processing steps (fermentation/expression,

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Section: Nonionic Surfactantsmentioning

confidence: 99%

External Factors Affecting Protein Aggregation

Wang

Speaker

2010

Aggregation of Therapeutic Proteins

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“…[9,10] It has been shown that incorporation of <1% (w=w) nonionic surfactant helps in protecting protein from denaturation during spray. [9,18] When a feed containing protein and surfactant is atomized, it outcompetes proteins in occupying the air-water interface, thus preventing proteins from reaching and unfolding at the air-water interface. Low-molecular-weight surfactants such as polysorbate-80 (Tween-80) have kinetic advantages over proteins to occupy the air-water interface due to their small size and faster diffusion speed.…”

Section: Introductionmentioning

confidence: 99%

Denaturation and Physical Characteristics of Spray-Dried Whey Protein Isolate Powders Produced in the Presence and Absence of Lactose, Trehalose, and Polysorbate-80

et al. 2015

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The denaturation (loss of protein through aggregation and/or change in secondary structure) and physical characteristics such as powder morphology, particle size and size distribution, amorphous/crystalline behavior, and solubility of whey protein isolate (WPI) were investigated in a spray-drying process. The protective efficacy of sugars (lactose and trehalose) and low-molecular-weight surfactant polysorbate-80 (Tween-80) on the secondary structure (b-turn, b-sheet and a-helix) and physical characteristics of spray-dried WPI was quantified. The WPI, WPIþsugar, and WPIþTween-80 formulations were spray dried maintaining the total solids at 10% (w/w). The inlet and outlet temperatures were maintained at 180 and 80 C, respectively. The results showed that the loss of protein through denaturation and aggregation was not significant (p > 0.05). However, a significant (p < 0.05) alteration of the secondary structural elements was observed. Due to spray drying of WPI without protectants, the b-sheet and b-turn were decreased by 4.4 and 14.5%, respectively, and the random coil increased by 20.7%. The a-helix of WPI remained unaltered during the spray-drying process. The presence of Tween-80 effectively protected the a-helix and b-sheet but the b-turn remained vulnerable and was decreased. No significant (p > 0.05) change in the solubility of WPI was observed due to spray drying. Spray drying of WPIþsugar produced essentially amorphous particles. The dried powder particles were spherical with wrinkled or folded surface.

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“…In addition, we investigated the time and temperature dependent fluorescence quenching behavior under a fixed concentration of clay and protein. A temperature of 60 • C was chosen as it was known that thermal aggregation begins at around this temperature [46,47], and thus we might see clay-protein interactions in different aspects through a temperature dependent study. As shown in Figure 6a, the protein itself did not show any fluorescence quenching at 25 • C. Under the presence of clays, the quenching ratio increased up to 30% and the order was the same as the magnitude of the values.…”

Section: Protein Fluorescence Quenchingmentioning

confidence: 99%

Physico–Chemical Interaction between Clay Minerals and Albumin Protein according to the Type of Clay

Kim

2019

Minerals

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Clay minerals are widely utilized in pharmaceutical and dermatological sciences as a gastrointestinal medicine or skin remediation agent. In order to verify the feasibility of clays as an injection, pill, or topical agent, it is important to study their interactions with biological components, such as proteins. In this study, we utilized a protein fluorescence quenching assay and circular dichroism spectroscopy to evaluate general aspects of protein denaturation and conformational change, respectively. Three different clays; layered double oxide (LDO), montmorilonite (MMT) and halloysite nanotube (HNT), were treated with albumin and the physico-chemical effect on the protein’s conformation was investigated. MMT was shown to influence the conformational change the most, owing to the large accessible adsorption site. HNT showed meaningful circular dichroism (CD) band collapse as well as fluorescence quenching in the protein, suggesting a potential harmful effect of HNT toward the protein. Among the three tested clays, LDO was determined to affect protein structure the least in terms of three-dimensional conformation and helical structure.

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Protection of Bovine Serum Albumin from Aggregation by Tween 80

Cited by 86 publications

References 16 publications

External Factors Affecting Protein Aggregation

External Factors Affecting Protein Aggregation

Denaturation and Physical Characteristics of Spray-Dried Whey Protein Isolate Powders Produced in the Presence and Absence of Lactose, Trehalose, and Polysorbate-80

Physico–Chemical Interaction between Clay Minerals and Albumin Protein according to the Type of Clay

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