Correlation of the CTD structural domain of hepatitis B virus core protein with the encapsulation effect of indocyanine green.

Yamin Wei; Yulin LI; Heng Zhang; Yiqing Zhang; Xiaojun Wang; Huirui Wang; Pengli Xiao; Peng Qian; Lei Ren; Yunlong Wang

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Correlation of the CTD structural domain of hepatitis B virus core protein with the encapsulation effect of indocyanine green.

Author: Yamin WEI ¹ ; Yulin LI ² ; Heng ZHANG ³ ; Yiqing ZHANG ⁴ ; Xiaojun WANG ³ ; Huirui WANG ⁵ ; Pengli XIAO ⁵ ; Peng QIAN ³ ; Lei REN ⁶ ; Yunlong WANG ¹
Author Information

1. School of Life Sciences, Zhengzhou University, Zhengzhou 450006, Henan, China.
2. Henan Bioengineering Technology Research Center, Zhengzhou 450000, Henan, China.
3. Henan General Hospital, Zhengzhou 450006, Henan, China.
4. Zhengzhou Technical College, Zhengzhou 450052, Henan, China.
5. Luoyang Central Hospital Affiliated to Zhengzhou University, Luoyang 471000, Henan, China.
6. Xiamen University, Xiamen 361005, Fujian, China.
Publication Type:Journal Article
Keywords: in vivo imaging; encapsulation efficiency; hepatitis B virus core protein; indocyanine green; polyarginine domain
MeSH: Animals; Hepatitis B/drug therapy*; Hepatitis B Core Antigens; Indocyanine Green/chemistry*; Mice; Nanoparticles/chemistry*; Viral Core Proteins
From: Chinese Journal of Biotechnology 2022;38(3):1039-1049
CountryChina
Language:Chinese
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.