Reactive molecular dynamics simulations investigating ROS-mediated HIV damage from outer gp120 protein to internal capsid protein.

Molecular dynamics (MD) with the ReaxFF force field is used to study the structural damage to HIV capsid protein and gp120 protein mediated by reactive oxygen species (ROS). Our results show that with an increase in ROS concentration, the structures of the HIV capsid protein and gp120 protein are more severely damaged, including dehydrogenation, increase in oxygen-containing groups, helix shortening or destruction, and peptide bond breaking. In particular, we noticed that extraction of H atoms from N atoms by ROS was significantly higher than that from C atoms. There was no significant difference in the effect of ROS on dehydrogenation and shortening or breaking of the helices. In contrast, the impact of O on the increase in oxygen-containing groups and the fracture of peptide bonds in the gp120 protein is more significant than that of O, and the effect of O is greater than that of ˙OH. In addition, the degree of structural damage of the gp120 protein was greater than that of the capsid protein. These detailed findings deepen our understanding of the role of ROS in regulating the structure and function of the HIV capsid protein and gp120 protein and provide valuable insights for plasma therapy for acquired immune deficiency syndrome (AIDS).