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The Covid-19 pandemic is driving research on the SARS-CoV-2 virus to find vaccines and treatments. Synthetic peptides are playing a big role in developing vaccines. C. Hyun-Jung Lee and H. Koohy at the University of Oxford have used in silico methods to identify 63 peptides as potential vaccine targets. They selected peptides that had a high degree of similarity to immunogenic peptides from SARS-CoV or to other immunogenic peptides in the Immune Epitope Database. These peptides provide a quick starting point in the search for a vaccine. A group at the University of Pittsburgh Medical Center have used recombinant proteins delivered into the skin by a unique microneedle array. When tested in mice, the vaccine produces antibodies specific to the SARS-CoV-2 virus in quantities believed to be sufficient to neutralize the virus.
In addition to vaccines, peptides are also being investigated as therapeutics to treat or prevent infection with the SARS-CoV-2 virus. Following the outbreaks of SARS-CoV and MERS-CoV, researchers in Shanghai have previously developed EK1, a pan-coronavirus fusion inhibiting peptide. EK1 is an optimized form of a peptide derived from the heptad repeat 2 domain of human CoV-OC43 strain and exhibits broad fusion inhibitory activity against many human corona viruses (HCoVs). Intranasal application of this peptide protected mice from HCoV-OC43 or MERS-CoV infection, which suggested that it could also have prophylactic and therapeutic applications with SARS-CoV-2. Subsequent studies verified that EK1 could significantly inhibit infection in ACE2 espressing 293T cells.
The Shanghai group has recently reported that linking cholesterol through a PEG4 linker to the C-terminal of EK1 produced a product (EK1C4) with potent inhibitory activity against SARS-CoV-2. The cholestrol-linked EK1 has 149-fold stronger activity than the original peptide. Mice receiving EK1C4 by intranasal application are protected from infection up to 12 hours. Results of post-infection treatment suggest that EK1C4 may have good therapeutic effect.
Researchers at MIT are also investigating SARS-CoV-2 fusion inhibiting peptides. Observing that the ACE2 peptidase domain α1 helix is important for binding SARS-CoV-2, they synthesized a 23 amino acid segment and a shorter truncated sequence. They report that the larger peptide has binding affinity comparable to full length ACE2 while the smaller peptide does not associate with receptor binding domain of SARS-CoV-2. The MIT team is studying the antiviral activity of the 23-aa peptide in mammalian cell cultures and are investigating potential optimizations.