We investigated the effects of KL 4, a 21-residue amphipathic peptide approximating the overall ratio of positively charged to hydrophobic amino acids in surfactant protein B (SP-B), on the structure and collapse of dipalmitoylphosphatidylcholine and palmitoyl-oleoyl-phosphatidylglycerol monolayers. As reported in prior work on model lung surfactant phospholipid films containing SP-B and SP-B peptides, our experiments show that KL 4 improves surfactant film reversibility during repetitive interfacial cycling in association with the formation of reversible collapse structures on multiple length scales. Emphasis is on exploring a general mechanistic connection between peptide-induced nano- and microscale reversible collapse structures (silos and folds). © 2011 Biophysical Society.
Holten-Andersen, N., Michael Henderson, J., Walther, F. J., Waring, A. J., Ruchala, P., Notter, R. H., & Lee, K. Y. C. (2011). KL 4 peptide induces reversible collapse structures on multiple length scales in model lung surfactant. Biophysical Journal, 101(12), 2957–2965. https://doi.org/10.1016/j.bpj.2011.10.050