KL₄ peptide induces reversible collapse structures on multiple length scales in model lung surfactant.
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).
Department of Chemistry, Institute for Biophysical Dynamics, and the James Franck Institute, University of Chicago, Chicago, Illinois, USA.
Niels
N
Holten-Andersen
J
J
Michael Henderson
Frans J
FJ
Walther
Alan J
AJ
Waring
Piotr
P
Ruchala
Robert H
RH
Notter
Ka Yee C
KY
Lee
D003198:Computer Simulation; D057927:Hydrophobic and Hydrophilic Interactions; D008168:Lung / Q000737:chemistry*; D008956:Models, Chemical; D008958:Models, Molecular; D010455:Peptides / Q000737:chemistry*; D011487:Protein Conformation; D011489:Protein Denaturation; D037701:Pulmonary Surfactant-Associated Protein B / Q000737:chemistry* / Q000648:ultrastructure*; D013499:Surface Properties
D010455:Peptides; D037701:Pulmonary Surfactant-Associated Protein B