KL4 Peptide Induces Reversible Collapse Structures on Multiple Length Scales in Model Lung Surfactant |
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| Authors: | Niels Holten-Andersen J Michael Henderson Frans J Walther Alan J Waring Piotr Ruchala Robert H Notter Ka Yee C Lee |
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| Institution: | †Department of Chemistry, Institute for Biophysical Dynamics, and the James Franck Institute, University of Chicago, Chicago, Illinois;‡Los Angeles Biomedical Research Institute at Harbor-UCLA Medical Center, Torrance, California;§Department of Pediatrics, Leiden University Medical Center, Leiden, The Netherlands;¶Department of Medicine, School of Medicine, University of California, Los Angeles, California;‖Department of Physiology and Biophysics, School of Medicine, University of California, Irvine, California;∗∗Department of Pediatrics, University of Rochester School of Medicine, Rochester, New York;††Department of Environmental Medicine, University of Rochester School of Medicine, Rochester, New York |
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| Abstract: | We investigated the effects of KL4, 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 KL4 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). |
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