RESUMO
Surfactant protein C (SP-C) is known to be essential for lung function and the formation of a surface confined reservoir at the alveolar interface. The structural features relevant for the peptide's extraordinary ability to form extended three-dimensional structures were systematically investigated and are summarized in the present paper. The influence of palmitoylation was studied for full length SP-Cs as well as truncated variants with the N-terminal residues 1-17 and 1-13, respectively. The combined results from film balance measurements, fluorescence microscopy (FLM) and scanning force microscopy (SFM) reveal a fine-tuned balance between the influence of the palmitoyl chains and alpha-helical length. Native SP-C added to DPPC/DPPG monolayers (molar ratio 80:20) induced the formation of the surface confined reservoir independent of its palmitoylation degree. However, topographic images revealed that only bilayers and not multilayers where formed when the acyl chains were missing. The influence of palmitoylation increased when alpha-helical length was considerably reduced to 17 or even 13 amino acid residues. In these strongly truncated SP-C peptides palmitoyl chains increased monolayer stability and anchored the peptides in the lipid film. However, no multilayer formation was observed at all for all shortened peptides. The alpha-helix of SP-C seems to be a prerequisite for the formation of extended three-dimensional structures and obviously has to be able to span a lipid bilayer. Palmitoylation obviously mediates interactions between lipids and/or peptides not only within a protein/lipid film but also between neighbouring layers and induces a stacking of bilayers.