Correlation of the CTD structural domain of hepatitis B virus core protein with the encapsulation effect of indocyanine green / 生物工程学报
Chinese Journal of Biotechnology
; (12): 1039-1049, 2022.
Article
em Zh
| WPRIM
| ID: wpr-927761
Biblioteca responsável:
WPRO
ABSTRACT
Hepatitis B virus core protein (HBc) has become a hot spot in drug carrier protein research due to its natural particle self-assembly ability and ease of modification. The truncation of the C-terminal polyarginine domain (CTD, aa 151-183) of HBc does not affect the self-assembly of the particles. However, it does affect the internal and external charges of the particles, which may subsequently affect drug encapsulation. Thus, the truncated C-terminal polyarginine domain (CTD) of HBc and the inserted RGD peptide were selected to construct and express three HBc variants (RH) encapsulated with ICG (RH/ICG) with different C-terminal lengths to compare the stability and drug activity of their nanoformulations. RH160/ICG was found to have a great advantages in encapsulation efficiency and biological imaging. Compared with other HBc variants, RH160/ICG significantly improved encapsulation efficiency, up to 32.77%±1.23%. Cytotoxicity and hemolysis assays further demonstrated the good biocompatibility of RH160/ICG. Cell uptake and in vivo imaging experiments in mice showed that RH160/ICG could efficiently deliver ICG in tumor cells and tumor sites with good imaging effect. This research provides a new direction for further expanding the diagnosis and treatment application of ICG and development of HBc-based nanoparticle drug carrier platform.
Palavras-chave
Texto completo:
1
Índice:
WPRIM
Assunto principal:
Proteínas do Core Viral
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Nanopartículas
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Hepatite B
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Antígenos do Núcleo do Vírus da Hepatite B
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Verde de Indocianina
Limite:
Animals
Idioma:
Zh
Revista:
Chinese Journal of Biotechnology
Ano de publicação:
2022
Tipo de documento:
Article