Short Helix-Constrained Peptides As RSV Fusion Inhibitors And Vaccine Candidates

TL;DRAbstract

Proteins frequently mediate their functions through small folded secondary structural motifs, such as α-helices accounting for >30% of protein structure. When such helices are sufficiently solvent-exposed, they can be recognized by other proteins and these protein- protein interactions are responsible for mediating infection, disease and human physiology. If these important helical epitopes could be recreated in short constrained peptides, they might be able to mimic both the structure and function of protein. Constraining peptides can also improve stability in biological media by decreasing proteolytic degradation. Short, chemically stable, peptide antigens that display key structural and functional properties of protein antigens may be suitable as vaccines or anti-viral drug candidates, being cheaper to make than proteins, safer to use than conventional pathogen-based vaccines, and easier to purify than proteins or pathogens. However, a number of obstacles need to be overcome in d

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