Stability of SIV gp32 Fusion‐Peptide Single‐Layer Protofibrils as Monitored by Molecular‐Dynamics Simulations

Abstract

Modeling the mechanisms of protofibril twisting: Molecular-dynamics simulations of simian viral peptide aggregates show that β sheets of 10 to 30 chains form left-handed helical ribbons with saddlelike curvature (see picture). These structures are highly dynamic, with oscillations around an average twist angle of 9–10°, and a pitch of 15–20 nm, depending on β-sheet length. The peptides studied are key to viral entry into host cells.