Optimal Hydrophobicity and Reorientation of Amphiphilic Peptides Translocating through Membrane.

ABSTRACT: Cell-penetrating and some antimicrobial peptides can translocate across lipid bilayers without disrupting the membrane structure. However, the molecular properties required for efficient translocation are not fully understood. We employed the Metropolis Monte Carlo method together with coarse-grained models to systematically investigate free-energy landscapes associated with the translocation of secondary amphiphilic peptides. We studied α-helical peptides with different length, amphiphilicity, and distribution of hydrophobic content and found a common translocation path consisting of adsorption, tilting, and insertion. In the adsorbed state, the peptides are parallel to the membrane plane, whereas, in the inserted state, the peptides are perpendicular to the membrane. Our simulations demo

SUBMITTER: Kabelka I 

PROVIDER: S-EPMC6139821 | biostudies-literature | 2018 Sep

REPOSITORIES: biostudies-literature