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Relevant bibliographies by topics / Protein stabilizer

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Journal articles

Academic literature on the topic 'Protein stabilizer'

Author: Grafiati

Published: 9 September 2021

Last updated: 12 February 2022

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Journal articles on the topic "Protein stabilizer"

1

Elmowafy, Mohammed, Nabil K. Alruwaili, Khaled Shalaby, et al. "Long-Acting Paliperidone Parenteral Formulations Based on Polycaprolactone Nanoparticles; the Influence of Stabilizer and Chitosan on In Vitro Release, Protein Adsorption, and Cytotoxicity." Pharmaceutics 12, no. 2 (2020): 160. http://dx.doi.org/10.3390/pharmaceutics12020160.

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Long-acting preparations containing the antipsychotic paliperidone for intramuscular injection has drawn considerable attention to achieve harmless long-term treatment. This study aimed to develop paliperidone loaded polycaprolactone (PCL) nanoparticles and investigate the influence of PCL/drug ratio, stabilizer type, and chitosan coating on physicochemical properties, protein adsorption, and cellular toxicity. Results showed that chitosan coating produced enlarged particle sizes, shifted the surface charges from negative into positive and did not influence encapsulation efficiencies. Chitosan coating relatively sustained the drug release especially in pluronic stabilized formulations. Pluronic F127 based formulations exhibited the least protein adsorption (384.3 μg/mL). Chitosan coating of Tween 80 and polyvinyl alcohol stabilized formulations significantly (p < 0.05) increased protein adsorption. Cellular viability was concentration-dependent and negatively affected by stabilizers. All formulations did not show cellular death at 1.56 μg/mL. Inflammatory responses and oxidative stress were less affected by Tween 80 compared with other stabilizers. Chitosan minimized all aspects of cellular toxicity. Collectively, stabilizer type and chitosan coating play critical roles in developing safe and effective long-acting PCL nanoparticles intended for parenteral drug delivery. The coated formulations containing Tween 80 and Pluronic F127 as stabilizers are warranted a future in vivo study to delineate its safety and efficacy profiles.

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2

McLaren, R. S., N. Caruccio, and J. Ross. "Human La protein: a stabilizer of histone mRNA." Molecular and Cellular Biology 17, no. 6 (1997): 3028–36. http://dx.doi.org/10.1128/mcb.17.6.3028.

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Histone mRNA is destabilized at the end of S phase and in cell-free mRNA decay reaction mixtures supplemented with histone proteins, indicating that histones might autoregulate the histone mRNA half-life. Histone mRNA destabilization in vitro requires three components: polysomes, histones, and postpolysomal supernatant (S130). Polysomes are the source of the mRNA and mRNA-degrading enzymes. To investigate the role of the S130 in autoregulation, crude S130 was fractionated by histone-agarose affinity chromatography. Two separate activities affecting the histone mRNA half-life were detected. The histone-agarose-bound fraction contained a histone mRNA destabilizer that was activated by histone proteins; the unbound fraction contained a histone mRNA stabilizer. Further chromatographic fractionation of unbound material revealed only a single protein stabilizer, which was purified to homogeneity, partially sequenced, and found to be La, a well-characterized RNA-binding protein. When purified La was added to reaction mixtures containing polysomes, a histone mRNA decay intermediate was stabilized. This intermediate corresponded to histone mRNA lacking 12 nucleotides from its 3' end and containing an intact coding region. Anti-La antibody blocked the stabilization effect. La had little or no effect on several other cell cycle-regulated mRNAs. We suggest that La prolongs the histone mRNA half-life during S phase and thereby increases histone protein production.

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3

Balasubramaniyam, Thananjeyan, Takumi Ishizuka, Chao-Da Xiao, Hong-Liang Bao, and Yan Xu. "2′-O-Methyl-8-methylguanosine as a Z-Form RNA Stabilizer for Structural and Functional Study of Z-RNA." Molecules 23, no. 10 (2018): 2572. http://dx.doi.org/10.3390/molecules23102572.

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In contrast to Z-DNA that was stabilized and well-studied for its structure by chemical approaches, the stabilization and structural study of Z-RNA remains a challenge. In this study, we developed a Z-form RNA stabilizer m8Gm, and demonstrated that incorporation of m8Gm into RNA can markedly stabilize the Z-RNA at low salt conditions. Using the m8Gm-contained Z-RNA, we determined the structure of Z-RNA and investigated the interaction of protein and Z-RNA.

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4

David, Shlomit, Maya Magram Klaiman, Avi Shpigelman, and Uri Lesmes. "Addition of Anionic Polysaccharide Stabilizers Modulates In Vitro Digestive Proteolysis of a Chocolate Milk Drink in Adults and Children." Foods 9, no. 9 (2020): 1253. http://dx.doi.org/10.3390/foods9091253.

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There is a need to better understand the possible anti-nutritional effect of food stabilizers on the digestibility of important macronutrients, like proteins. This study hypothesized that the anionic nature of κ-, ι-, λ-, Carrageenan (CGN) and xanthan gum directs their interactions with food proteins leading to their subsequent attenuated digestive proteolysis. Model chocolate milk drinks were tested for their colloidal properties, viscosity and proteolytic breakdown in adults and children using in vitro digestion models coupled with proteomic analyses. SDS-PAGE analyses of gastro-intestinal effluents highlight stabilizers hinder protein breakdown in adults and children. Zeta potential and colloidal particle size were the strongest determinants of stabilizers’ ability to hinder proteolysis. LC-MS proteomic analyses revealed stabilizer addition significantly reduced bioaccessibility of milk-derived bioactive peptides with differences in liberated peptide sequences arising mainly from their location on the outer rim of the protein structures. Further, liberation of bioactive peptides emptying from a child stomach into the intestine were most affected by the presence of ι-CGN. Overall, this study raises the notion that stabilizer charge and other properties of edible proteins are detrimental to the ability of humans to utilize the nutritional potential of such formulations. This could help food professionals and regulatory agencies carefully consider the use of anionic stabilizers in products aiming to serve as protein sources for children and other liable populations.

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5

Milroy, Lech-Gustav, Maria Bartel, Morkos A. Henen, et al. "Stabilizer-Guided Inhibition of Protein-Protein Interactions." Angewandte Chemie 127, no. 52 (2015): 15946–50. http://dx.doi.org/10.1002/ange.201507976.

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6

Milroy, Lech-Gustav, Maria Bartel, Morkos A. Henen, et al. "Stabilizer-Guided Inhibition of Protein-Protein Interactions." Angewandte Chemie International Edition 54, no. 52 (2015): 15720–24. http://dx.doi.org/10.1002/anie.201507976.

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7

Serdar Akin, M., Busra Goncu, and Mutlu B. Akin. "Designing an industrial protocol to develop a new fat-reduced- ice cream formulation by replacing stabilizers with microbial transglutaminase enzyme." Mljekarstvo 69, no. 3 (2019): 162–71. http://dx.doi.org/10.15567/mljekarstvo.2019.0302.

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In this study, the possibility of replacing stabilizers with microbial transglutaminase (MTG) enzyme in fat-reduced ice cream production was studied. In addition, the stage of adding (before or after the heat treatment) the MTG enzyme to ice cream was also investigated. Five different ice creams (A and C containing 1 unit MTG/g protein without stabilizer, B and D containing 0.5 unit MTG/g protein and 0.35 % stabilizer, which also consist of the mixture of Carrageenan (E 407), Guar gum (E 412), Xanthan gum (E 415) and Sodium alginate (E 401), and E (control) containing 0.7 % stabilizer) were manufactured. MTG has been added to samples A and B after heat treatment while it was added to C and D samples before the heat treatment. An experimental analysis related to the overrun, viscosity melting properties, pH, titratable acidity, dry matter, fat, protein, sensorial and microstructural properties of ice creams was carried out. According to the results, the amount and the adding stage of MTG significantly affected overrun, melting, viscosity, coldness, firmness, smoothness, mouth coating, color, appearance, taste, smell scores, and also microstructure of ice creams (p&lt;0.01). Results also showed that MTG could be used together with other stabilizers after heat treatment in the production of ice cream. Moreover, our findings demonstrated that sample B was the closest to control in terms of sensorial properties.

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Kaushik, Jai K., and Rajiv Bhat. "Why Is Trehalose an Exceptional Protein Stabilizer?" Journal of Biological Chemistry 278, no. 29 (2003): 26458–65. http://dx.doi.org/10.1074/jbc.m300815200.

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9

Majumder, Manna. "Depolymerized Chitosan: A Novel Milk Protein Stabilizer." Advances in Bioscience and Bioengineering 3, no. 6 (2015): 56. http://dx.doi.org/10.11648/j.abb.20150306.11.

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10

Diana, Jebun Nessa, Ying Tao, Qiran Du, et al. "PLGA Microspheres of hGH of Preserved Native State Prepared Using a Self-Regulated Process." Pharmaceutics 12, no. 7 (2020): 683. http://dx.doi.org/10.3390/pharmaceutics12070683.

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The challenges of formulating recombinant human growth hormone (rhGH) into sustained-release polymeric microspheres include two mutual causal factors, protein denaturing by the formulation process and severe initial burst release related with relative high dose. The stabilizers to protect the proteins must not evoke osmotic pressure inside the microspheres, and the contact of the protein with the interface between water and organic solution of the polymer must be minimized. To meet these criteria, rhGH was pre-formulated into polysaccharide particles via an aqueous–aqueous emulsion in the present study, followed by encapsulating the particles into microspheres through a self-regulated process to minimize the contact of the protein with the water–oil interface. Polysaccharides as the protein stabilizer did not evoke osmotic pressure as small sugar stabilizers, the cause of severe initial burst release. Reduced initial burst enabled reduced protein loading to 9% (from 22% of the once commercialized Nutropin depot), which in turn reduced the dosage form index from 80 to 8.7 and eased the initial burst. A series of physical chemical characterizations as well as biologic and pharmacokinetic assays confirmed that the present method is practically feasible for preparing microspheres of proteins.

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