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Viroporins are small viral proteins that oligomerize in the membrane of hostcells and induce the formation of hydrophilic pores in these membranes, thusaltering the physiological properties of the host cells. Due to theirsignificance for viral pathogenicity, they have become targets forpharmaceutical intervention, especially through compounds that block theirpore-forming activity. Here we add to the growing literature concerning thestructure and function of viroporins by studying and comparing -- throughmolecular dynamics simulations -- the folding of the transmembrane domainpeptides of viroporins derived from four viruses : influenza A, influenza B,and the coronaviruses MERS-Cov-2 and SARS-CoV-2. Through a total of more than50 {\mu}s of simulation time in explicit solvent (TFE) and with fullelectrostatics, we characterize the folding behavior, helical stability andhelical propensity of these transmembrane peptides in their monomeric state andwe identify common motifs that may reflect their quaternary organization and/orbiological function. We show that the two influenza-derived peptides aresignificantly different in peptide sequence and secondary structure from thetwo coronavirus-derived peptides, and that they are organized in twostructurally distinct parts : a significantly more stable N-terminal half, anda fast converting C-terminal half that continuously folds and unfolds between$\alpha$-helical structures and non-canonical structures which are mostlyturns. In contrast, the two coronavirus-derived transmembrane peptides are muchmore stable and fast helix formers when compared with the influenza ones. Wediscuss possible interpretations of these findings and their putativeconnection to the structural characteristics of the respective viroporins.

Folding Molecular Dynamics Simulations of the Transmembrane Peptides of Influenza A, B M2, and MERS-, SARS-CoV E Viral Proteins