Single Particle Analysis Reveals the Organization of the Membrane Remodeling Protein Caveolin-1 within Disc-Shaped Complexes

Abstract

adsorption of wild-typed HD5 (WT) and T7E21R on a bacterial membrane were conducted. A bacterial membrane models with O-antigen of lipopolysaccharides (LPS) mimicking E. coli membrane was used. Atomistic molecular simulations were performed to obtain an insight into the adsorption of these peptides on the bacterial membrane. Our data highlight the different dimeric conformation between WT and T7E21R. It is found that the parallel b-strands of T7E21R is formed instead of antiparallel in HD5. This conformation of change results in different degrees of binding affinities. Key interactions are also extracted here. However, it is shown that WT can penetrate deeper into the O-antigen than T7E21R. The uncharged residues such as Thr, Ser, Gly, and Tyr are dominated in contacts with O-antigen of LPS as much as the charged residues. An insight obtained here can serve as a guideline for further improvement of defensin-derived antibiotic design.