Preparation and brain targeting effects study of recombinant human ferritin nanoparticles.

Wang, Zhixian; Xu, Xiaoling; Zhu, Yunhuan; Qian, Yuncheng; Feng, Yilu; Li, Hongyu; Hu, Guoheng

Wang, Zhixian; Xu, Xiaoling; Zhu, Yunhuan; Qian, Yuncheng; Feng, Yilu; Li, Hongyu; Hu, Guoheng.

Afiliación

Wang Z; The First Clinical College of Traditional Chinese Medicine, Hunan University of Traditional Chinese Medicine, Changsha, 410208, China; First Affiliated Hospital of Hunan University of Chinese Medicine, Changsha, 410007, China.
Xu X; Shulan International Medical College, Zhejiang Shuren University, Hangzhou, 310015, China.
Zhu Y; Shulan International Medical College, Zhejiang Shuren University, Hangzhou, 310015, China.
Qian Y; Shulan International Medical College, Zhejiang Shuren University, Hangzhou, 310015, China.
Feng Y; Shulan International Medical College, Zhejiang Shuren University, Hangzhou, 310015, China.
Li H; Shulan International Medical College, Zhejiang Shuren University, Hangzhou, 310015, China.
Hu G; First Affiliated Hospital of Hunan University of Chinese Medicine, Changsha, 410007, China. Electronic address: huguoheng@hnucm.edu.cn.

Biochem Biophys Res Commun ; 712-713: 149939, 2024 Jun 18.

Article en En | MEDLINE | ID: mdl-38640729

ABSTRACT

ABSTRACT

Human heavy-chain ferritin is a naturally occurring protein with high stability and multifunctionality in biological systems. This study aims to utilize a prokaryotic expression system to produce recombinant human heavy-chain ferritin nanoparticles and investigate their targeting ability in brain tissue. The human heavy-chain ferritin gene was cloned into the prokaryotic expression vector pET28a and transformed into Escherichia coli BL21 (DE3) competent cells to explore optimal expression conditions. The recombinant protein was then purified to evaluate its immunoreactivity and characteristics. Additionally, the distribution of the administered protein in normal mice and its permeability in an in vitro blood-brain barrier (BBB) model were measured. The results demonstrate that the purified protein can self-assemble extracellularly into nano-cage structures of approximately 10 nm and is recognized by corresponding antibodies. The protein effectively penetrates the blood-brain barrier and exhibits slow clearance in mouse brain tissue, showing excellent permeability in the in vitro BBB model. This study highlights the stable expression of recombinant human heavy-chain ferritin using the Escherichia coli prokaryotic expression system, characterized by favorable nano-cage structures and biological activity. Its exceptional brain tissue targeting and slow metabolism lay an experimental foundation for its application in neuropharmaceutical delivery and vaccine development fields.

Asunto(s)

Barrera Hematoencefálica; Encéfalo; Escherichia coli; Ferritinas; Nanopartículas; Proteínas Recombinantes; Animales; Humanos; Proteínas Recombinantes/genética; Proteínas Recombinantes/metabolismo; Ratones; Barrera Hematoencefálica/metabolismo; Encéfalo/metabolismo; Escherichia coli/genética; Escherichia coli/metabolismo; Nanopartículas/química; Ferritinas/metabolismo; Ferritinas/genética; Ferritinas/química; Apoferritinas/metabolismo; Apoferritinas/genética; Apoferritinas/química; Distribución Tisular

Palabras clave

Brain-targeting nanomaterials; Human heavy-chain ferritin; Inclusion body purification; Prokaryotic expression; Protein refolding

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Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Encéfalo / Proteínas Recombinantes / Barrera Hematoencefálica / Escherichia coli / Nanopartículas / Ferritinas Límite: Animals / Humans Idioma: En Revista: Biochem Biophys Res Commun Año: 2024 Tipo del documento: Article País de afiliación: China Pais de publicación: Estados Unidos

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