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可变热条件下制备的磁铁蛋白的氧化还原、水解和脱水化学对其结构和磁性能的影响。

The Impact of Redox, Hydrolysis and Dehydration Chemistry on the Structural and Magnetic Properties of Magnetoferritin Prepared in Variable Thermal Conditions.

机构信息

Institute of Hydrology SAS, Dúbravská Cesta 9, 84104 Bratislava, Slovakia.

Institute of Materials Research Slovak Academy of Sciences, Watsonova 47, 04001 Košice, Slovakia.

出版信息

Molecules. 2021 Nov 18;26(22):6960. doi: 10.3390/molecules26226960.

DOI:10.3390/molecules26226960
PMID:34834056
原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC8619319/
Abstract

Ferritin, a spherically shaped protein complex, is responsible for iron storage in bacteria, plants, animals, and humans. Various ferritin iron core compositions in organisms are associated with specific living requirements, health state, and different biochemical roles of ferritin isomers. Magnetoferritin, a synthetic ferritin derivative, serves as an artificial model system of unusual iron phase structures found in humans. We present the results of a complex structural study of magnetoferritins prepared by controlled in vitro synthesis. Using various complementary methods, it was observed that manipulation of the synthesis technology can improve the physicochemical parameters of the system, which is useful in applications. Thus, a higher synthesis temperature leads to an increase in magnetization due to the formation of the magnetite phase. An increase in the iron loading factor has a more pronounced impact on the protein shell structure in comparison with the pH of the aqueous medium. On the other hand, a higher loading factor at physiological temperature enhances the formation of an amorphous phase instead of magnetite crystallization. It was confirmed that the iron-overloading effect alone (observed during pathological events) cannot contribute to the formation of magnetite.

摘要

铁蛋白是一种球形蛋白质复合物,负责细菌、植物、动物和人类的铁储存。生物体中各种铁蛋白铁核组成与特定的生活需求、健康状态以及铁蛋白异构体的不同生化作用有关。磁铁蛋白是一种合成铁蛋白衍生物,可用作在人类中发现的异常铁相结构的人工模型系统。我们介绍了通过体外控制合成制备的磁铁蛋白的复杂结构研究结果。使用各种互补方法,观察到合成技术的操纵可以改善系统的物理化学参数,这在应用中很有用。因此,较高的合成温度会由于形成磁铁矿相而导致磁化增加。与水介质的 pH 值相比,铁负载因子的增加对蛋白质壳结构的影响更为显著。另一方面,在生理温度下较高的负载因子会增强非晶相的形成,而不是磁铁矿的结晶。已经证实,仅铁过载效应(在病理事件中观察到)不能促成磁铁矿的形成。

https://cdn.ncbi.nlm.nih.gov/pmc/blobs/7706/8619319/b3c515c9ebf5/molecules-26-06960-g008.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/7706/8619319/9ab0815fc3e7/molecules-26-06960-g001.jpg
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https://cdn.ncbi.nlm.nih.gov/pmc/blobs/7706/8619319/d767065939ca/molecules-26-06960-g003.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/7706/8619319/5c2adf058d8a/molecules-26-06960-g004.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/7706/8619319/bdf57cfe5957/molecules-26-06960-g005.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/7706/8619319/f37b14aa3827/molecules-26-06960-g006.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/7706/8619319/87851de09363/molecules-26-06960-g007.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/7706/8619319/b3c515c9ebf5/molecules-26-06960-g008.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/7706/8619319/9ab0815fc3e7/molecules-26-06960-g001.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/7706/8619319/86db949b0f27/molecules-26-06960-g002.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/7706/8619319/d767065939ca/molecules-26-06960-g003.jpg
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https://cdn.ncbi.nlm.nih.gov/pmc/blobs/7706/8619319/bdf57cfe5957/molecules-26-06960-g005.jpg
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https://cdn.ncbi.nlm.nih.gov/pmc/blobs/7706/8619319/b3c515c9ebf5/molecules-26-06960-g008.jpg

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