Molecular dynamics study of the lung surfactant peptide SP-B1-25 with DPPC monolayers: insights into interactions and peptide position and orientation.

ABSTRACT: We have performed molecular dynamics simulations of the interactions of the peptide SP-B(1-25), which is a truncated version of the full pulmonary surfactant protein SP-B, with dipalmitoylphosphatidylcholine monolayers, which are the major lipid components of lung surfactant. Simulations of durations of 10-20 ns show that persistent hydrogen bonds form between the donor atoms of the protein and the acceptors of the lipid headgroup and that these bonds determine the position, orientation, and secondary structure of the peptide in the membrane environment. From an ensemble of initial conditions, the most probable equilibrium orientation of the alpha-helix of the peptide is predicted to be parallel to the interface, matching recent experimental results on model lipid mixtures. Simulations of

SUBMITTER: Kandasamy SK 

PROVIDER: S-EPMC1305215 | biostudies-literature | 2005 Mar

REPOSITORIES: biostudies-literature