Identification of aptamer-binding sites in hepatitis C virus envelope glycoprotein E2

Fan Chen, Si Chong Chen, Jing Zhou, Zhi De Chen, Fang Chen

Research output: Contribution to journalArticlepeer-review

3 Scopus citations


Hepatitis C Virus (HCV) encodes two envelope glycoproteins, E1 and E2. Our previous work selected a specific aptamer ZE2, which could bind to E2 with high affinity, with a great potential for developing new molecular probes as an early diagnostic reagents or therapeutic drugs targeting HCV. In this study, the binding sites between E2 and aptamer ZE2 were further explored. E2 was truncated to 15 peptides (P1 to P15) and these peptides were used to detect the affinity with ZE2 by ELISA respectively. The peptide with high affinity was then further truncated, detected and compared with six kinds of HCV genotypes. The basic amino acid in 500 aa bound to ZE2 with high affinity, while acidic amino acid in 501 aa reduced the reaction between E2 and ZE2. The results showed the 500 aa and 501 aa of E2 were the key sites that bound to ZE2.

Original languageEnglish
Pages (from-to)63-67
Number of pages5
JournalIranian Journal of Medical Sciences
Issue number1
StatePublished - 1 Jan 2015
Externally publishedYes


  • Aptamer
  • Binding site
  • Glycoprotein E2
  • Hepatitis C virus

ASJC Scopus subject areas

  • Medicine (miscellaneous)
  • Biochemistry, Genetics and Molecular Biology (miscellaneous)
  • Immunology and Microbiology (miscellaneous)
  • Clinical Psychology
  • Pharmacology, Toxicology and Pharmaceutics (miscellaneous)


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