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Updated: Oct 2, 2025

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Published on: March 5, 2017
The interaction and orientation of Peptide KL4 in model membranes
Drew Marquardt1, Brad van Oosten2, Maksymilian Dziura3
1Department of Chemistry and Biochemistry, University of Windsor, Windsor, Ontario, Canada; Department of Physics, University of Windsor, Windsor, Ontario, Canada.
Abstract:
We report on the orientation and location of synthetic pulmonary surfactant peptide KL4, (KLLLL)4K, in model lipid membranes. The partitioning depths of selectively deuterated leucine residues within KL4 were determined in DPPC:POPG (4:1) and POPC:POPG (4:1) bilayers by oriented neutron diffraction. These measurements were combined with an NMR-generated model of the peptide structure to determine the orientation and partitioning of the peptide at the lipid-water interface. The results demonstrate KL4 adopting an orientation that interacts with a single membrane leaflet. These observations are consistent with past 2H NMR and EPR studies (Antharam et al., 2009; Turner et al., 2014).
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