TY - JOUR
T1 - Targeted Degradation of HCV Polymerase by GalNAc-Conjugated ApTACs for Pan-Genotypic Antiviral Therapy with High Resistance Barriers
AU - Pan, Wei
AU - Wu, Sijin
AU - Zhou, Honglin
AU - Xia, Yaodong
AU - Li, Qingchao
AU - Ge, Ruixin
AU - Wu, Jiaxuan
AU - Han, Han
AU - Chen, Song
AU - Li, Yan
AU - Li, Jingrui
AU - Chen, Miao
AU - Liu, Min
AU - Zhou, Jun
AU - Xie, Songbo
N1 - Publisher Copyright:
© 2025 American Chemical Society.
PY - 2025
Y1 - 2025
N2 - Hepatitis C virus (HCV) infection is a major cause of chronic liver disease. Although interferon-free direct-acting antivirals have led to significant advancements in the treatment of HCV infection, the high genetic variability of the virus and the emergence of acquired drug resistance pose potential threats to their effectiveness. In this study, we develop a broad-spectrum aptamer-based proteolysis targeting chimera, designated dNS5B, which effectively degrades both pan-genotypic NS5B polymerase and drug-resistant mutants through ubiquitin proteasome system. To achieve hepatocyte-specific uptake, we further develop Gal-dNS5B by coupling the dNS5B with a trivalent N-acetylgalactosamine (tri-GalNAc), a ligand for the liver-specific asialoglycoprotein receptor. Gal-dNS5B exclusively accumulates in hepatocytes and suppresses HCV replication by degrading NS5B. Collectively, our research lays the groundwork for a scalable strategy in the development of antiviral medications aimed at addressing current and future challenges posed by hepatitis viruses and other re-emerging viral pandemics.
AB - Hepatitis C virus (HCV) infection is a major cause of chronic liver disease. Although interferon-free direct-acting antivirals have led to significant advancements in the treatment of HCV infection, the high genetic variability of the virus and the emergence of acquired drug resistance pose potential threats to their effectiveness. In this study, we develop a broad-spectrum aptamer-based proteolysis targeting chimera, designated dNS5B, which effectively degrades both pan-genotypic NS5B polymerase and drug-resistant mutants through ubiquitin proteasome system. To achieve hepatocyte-specific uptake, we further develop Gal-dNS5B by coupling the dNS5B with a trivalent N-acetylgalactosamine (tri-GalNAc), a ligand for the liver-specific asialoglycoprotein receptor. Gal-dNS5B exclusively accumulates in hepatocytes and suppresses HCV replication by degrading NS5B. Collectively, our research lays the groundwork for a scalable strategy in the development of antiviral medications aimed at addressing current and future challenges posed by hepatitis viruses and other re-emerging viral pandemics.
UR - http://www.scopus.com/inward/record.url?scp=85214332110&partnerID=8YFLogxK
U2 - 10.1021/acs.jmedchem.4c02068
DO - 10.1021/acs.jmedchem.4c02068
M3 - Article
AN - SCOPUS:85214332110
SN - 0022-2623
JO - Journal of Medicinal Chemistry
JF - Journal of Medicinal Chemistry
ER -