![]() Stapling can be applied to enhance the alpha-helicity of peptides, which would otherwise adopt a random coil conformation in solution. Stapling involves such chemical modifications designed to constrain the peptide chain in the secondary structure of the native conformation, and the peptide products are known as stapled peptides. Because peptides can lose their shape when taken out of context, developing chemical interventions to stabilize their bioactive structure remains an active area of research. Loss of secondary structure usually means loss of biological function. Short peptides, when isolated from the parent protein, lose their secondary structure and exist in solution as unstructured, linear molecules. These stapled peptides, which mimic Helix 1 of the human ACE2 receptor, have demonstrated mixed ability to prevent infection with SARS-CoV-2 in cell-based studies. ![]() Several independent research initiatives have investigated the inhibitory effect of stapled peptides on binding of the severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2), the causative agent of COVID-19, to its receptor, angiotensin-converting-enzyme 2 (ACE2). The potential use of stapled peptides as inhibitors of viral entry, and therefore as antiviral therapeutics, has been established for several important viruses causing disease in humans, such as the human immunodeficiency virus type 1 (HIV-1), respiratory syncytial virus (RSV), and Middle East Respiratory Syndrome (MERS) coronavirus. Stapled peptides have been investigated as potential modulators of protein–protein interactions for over two decades. Stapled peptides are synthetic peptidomimetics of bioactive sites in folded proteins which carry chemical links, introduced during peptide synthesis, designed to retain the secondary structure in the native protein molecule.
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