دورية أكاديمية
Freeze-thaw-induced aggregation of bovine gamma globulin was efficiently inhibited by an intrinsically disordered plant protein dehydrin
| العنوان: | Freeze-thaw-induced aggregation of bovine gamma globulin was efficiently inhibited by an intrinsically disordered plant protein dehydrin |
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| المؤلفون: | Honami Osuda, Yuki Kimura, Masakazu Hara |
| المصدر: | Food Hydrocolloids for Health, Vol 3, Iss , Pp 100108- (2023) |
| بيانات النشر: | Elsevier, 2023. |
| سنة النشر: | 2023 |
| المجموعة: | LCC:Nutrition. Foods and food supply LCC:Nutritional diseases. Deficiency diseases |
| مصطلحات موضوعية: | Bovine gamma globulin, Cryoprotection, Dehydrin, Intrinsically disordered proteins, Protein aggregation, Nutrition. Foods and food supply, TX341-641, Nutritional diseases. Deficiency diseases, RC620-627 |
| الوصف: | Immunoglobulin, which is widely used in the formulation of protein drugs, is prone to aggregation due to freezing. The aggregated immunoglobulin exhibits decreased immune-reactivity and increasing immunogenicity. Accordingly, large amounts of excipients are added to immunoglobulin drugs to prevent aggregation. In the present study, we found that an Arabidopsis dehydrin (AtHIRD11), which is a stress-related intrinsically disordered protein, could efficiently inhibit the cryoaggregation of bovine gamma globulin (BGG). AtHIRD11 was 3 to 4 orders of magnitude more efficient than general protectants such as sugars and amino acids at the molar levels. The K-segment, which is a conserved sequence of dehydrin, was one of the protective sites of AtHIRD11. Amino acid substitution analysis indicated that the hydrophobic amino acids contributed to the cryoprotective activity of the K-segment. Moreover, the activity was roughly correlated with the hydropathy scores of hydrophobic amino acids. BGG and the K-segment individually migrated in size exclusion chromatography, showing that the K-segment did not bind to BGG in solution. This suggests that dehydrin may prevent the cryoaggregation of BGG via the K-segment through a transient hydrophobic interaction. Dehydrin may be utilized as an effective stabilizer of immunoglobulin to minimize aggregation under freezing conditions. |
| نوع الوثيقة: | article |
| وصف الملف: | electronic resource |
| اللغة: | English |
| تدمد: | 2667-0259 |
| Relation: | http://www.sciencedirect.com/science/article/pii/S2667025922000541; https://doaj.org/toc/2667-0259 |
| DOI: | 10.1016/j.fhfh.2022.100108 |
| URL الوصول: | https://doaj.org/article/01dd72222e7a40adb9b2b3046ebb761c |
| رقم الأكسشن: | edsdoj.01dd72222e7a40adb9b2b3046ebb761c |
| قاعدة البيانات: | Directory of Open Access Journals |
Full Text Finder | تدمد: | 26670259 |
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| DOI: | 10.1016/j.fhfh.2022.100108 |