Dimerized fusion inhibitor peptides targeting the HR1-HR2 interaction of SARS-CoV-2.
Kohei TsujiKofi Baffour-Awuah OwusuYutaro MiuraTakahiro IshiiKouki ShinoharaTakuya KobayakawaAkino EmiTakashi NakanoYouichi SuzukiHirokazu TamamuraPublished in: RSC advances (2023)
Membrane fusion is a critical and indispensable step in the replication cycles of viruses such as SARS-CoV-2 and human immunodeficiency virus type-1 (HIV-1). In this step, a trimer of the heptad repeat 1 (HR1) region interacts with the three HR2 regions and forms a 6-helix bundle (6-HB) structure to proceed with membrane fusion of the virus envelope and host cells. Recently, several researchers have developed potent peptidic SARS-CoV-2 fusion inhibitors based on the HR2 sequence and including some modifications. We have developed highly potent HIV-1 fusion inhibitors by dimerization of its HR2 peptides. Here, we report the development of dimerized HR2 peptides of SARS-CoV-2, which showed significantly higher antiviral activity than the corresponding monomers, suggesting that the dimerization strategy can facilitate the design of potent inhibitors of SARS-CoV-2.
Keyphrases
- sars cov
- human immunodeficiency virus
- antiretroviral therapy
- respiratory syndrome coronavirus
- hepatitis c virus
- hiv infected
- hiv positive
- hiv aids
- hiv testing
- induced apoptosis
- anti inflammatory
- drug delivery
- south africa
- men who have sex with men
- transcription factor
- cancer therapy
- cell cycle arrest
- oxidative stress
- signaling pathway
- binding protein
- cell proliferation
- pi k akt