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Liver cell-specific peptides derived from the preS1 domain of human hepatitis B virus

Kang, Jeong-Hun, Toita, Riki, Asai, Daisuke, Yamaoka, Tetsuji, Murata, Masaharu
Journal of virological methods 2014 v.201 pp. 20-23
Hepatitis B virus, amino acids, binding capacity, hepatocytes, hepatoma, human cell lines, humans, liver, pathogenicity, peptides, surface proteins
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.