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Molecular Dynamics Study of the Lung Surfactant Peptide SP-B_1–25 with DPPC Monolayers: Insights into Interactions and Peptide Position and Orientation

Chemical Engineering Department, The University of Michigan, Ann Arbor, Michigan

Correspondence: Address reprint requests to Ronald G. Larson, Chemical Engineering Department, University of Michigan, Ann Arbor, MI 48109. E-mail: rlarson{at}umich.edu.

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 -helix of the peptide is predicted to be parallel to the interface, matching recent experimental results on model lipid mixtures. Simulations of a few mutated analogs of SP-B_1–25 also suggest that the charged amino acids are important in determining the position of the peptide in the interface. The first eight amino acids of the peptide, also known as the insertion sequence, are found to be essential in reducing the fluctuations and anchoring the peptide in the lipid/water interface.

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