Abstract
Non-structural protein 3 (NS3) of hepatitis C virus (HCV) contains two distinct activities, protease and helicase which are essential for the HCV replication. In the previous study, we succeeded to obtain RNA aptamers, G9-I, G9-II and G9-III specific for the NS3 protease domain (delta NS3) by in vitro selection (1). As the result of mutational analysis in G9-I, we could obtain the minimum length of RNA structure, delta NEO-III maintaining the full inhibitional activity as shown in G9-I. Furthermore, we created a bi-functional novel RNA ligand, NEO-III-14U which was constructed by connecting delta NEO-III with (U)14 at the 3' terminal. NEO-III-14U was able to inhibit the unwinding of duplex DNA catalyzed by the Full-NS3 helicase activity as well as the protease activity in vitro. Consequently, we could obtain the dual-functional RNA ligand which could inhibit both NS3 protease and helicase activities essential for the HCV proliferation.
Sign-in/Register to access full text options 
Talk to us
Join us for a 30 min session where you can share your feedback and ask us any queries you have
Schedule a callDisclaimer: All third-party content on this website/platform is and will remain the property of their respective owners and is provided on "as is" basis without any warranties, express or implied. Use of third-party content does not indicate any affiliation, sponsorship with or endorsement by them. Any references to third-party content is to identify the corresponding services and shall be considered fair use under The CopyrightLaw.
