Department of Biomedical Engineering, National Cerebral and Cardiovascular Center Research Institute, 5-7-1 Fujishirodai, Suita, Osaka 565-8565, Japan.
Department of Biomaterials, Faculty of Dental Science, Kyushu University, 3-1-1 Maidashi, Higashi-ku, Fukuoka-shi, Fukuoka 812-8582, Japan.
J Virol Methods. 2014 Jun;201:20-3. doi: 10.1016/j.jviromet.2014.02.013. Epub 2014 Feb 22.
The envelope of human hepatitis B virus (HBV) consists of the large (L), middle (M), and small (S) surface proteins. The preS1 domain at the N terminus of the L-protein is essential for recognizing a target cell and for viral infectivity. In the present study, peptides derived from the preS1 domain (amino acid residues 2-19) were synthesized, and their binding affinities for human hepatocellular carcinoma (HCC) cells were determined. Non-myristoylated peptides showed much lower affinity for HepG2 cells than myristoylated peptides. Although all peptides showed significantly higher affinities for two human HCC cell lines (HepG2 and HuH-7) compared with other cell lines (HeLa, B16, NMuLi, and NIH 3T3), a modified peptide exhibited the highest affinity for HCC cell lines. These results suggest that the modified peptide can target liver cells.
乙型肝炎病毒(HBV)的包膜由大(L)、中(M)和小(S)表面蛋白组成。L 蛋白 N 端的前 S1 结构域对于识别靶细胞和病毒感染力是必需的。在本研究中,合成了来自前 S1 结构域(氨基酸残基 2-19)的肽,并测定了它们与人肝癌(HCC)细胞的结合亲和力。非豆蔻酰化肽与 HepG2 细胞的亲和力明显低于豆蔻酰化肽。虽然所有肽与其他细胞系(HeLa、B16、NMuLi 和 NIH 3T3)相比,对两种人 HCC 细胞系(HepG2 和 HuH-7)的亲和力显著更高,但修饰后的肽对 HCC 细胞系的亲和力最高。这些结果表明,修饰后的肽可以靶向肝细胞。