KL 4 peptide induces reversible collapse structures on multiple length scales in model lung surfactant

14Citations
Citations of this article
19Readers
Mendeley users who have this article in their library.

Abstract

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.

Cite

CITATION STYLE

APA

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

Register to see more suggestions

Mendeley helps you to discover research relevant for your work.

Already have an account?

Save time finding and organizing research with Mendeley

Sign up for free