The interaction and orientation of Peptide KL4 in model membranes

Drew Marquardt; Brad van Oosten; Maksymilian Dziura; Joanna R Long; Thad A Harroun

doi:10.1016/j.bbamem.2022.183893

The interaction and orientation of Peptide KL₄ in model membranes

Biochim Biophys Acta Biomembr. 2022 Jul 1;1864(7):183893. doi: 10.1016/j.bbamem.2022.183893. Epub 2022 Feb 25.

Authors

Drew Marquardt¹, Brad van Oosten², Maksymilian Dziura³, Joanna R Long⁴, Thad A Harroun⁵

Affiliations

¹ Department of Chemistry and Biochemistry, University of Windsor, Windsor, Ontario, Canada; Department of Physics, University of Windsor, Windsor, Ontario, Canada. Electronic address: drew.marquardt@uwindsor.ca.
² Department of Physics, Brock University, St. Catharines, Ontario, Canada.
³ Department of Chemistry and Biochemistry, University of Windsor, Windsor, Ontario, Canada.
⁴ Department of Biochemistry and Molecular Biology, University of Florida, Gainesville, FL, USA.
⁵ Department of Physics, Brock University, St. Catharines, Ontario, Canada. Electronic address: thad.harroun@brocku.ca.

PMID: 35219719
DOI: 10.1016/j.bbamem.2022.183893

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).

Keywords: KL(4); Lung surfactant; Membranes.

Publication types

Research Support, Non-U.S. Gov't

MeSH terms

Intercellular Signaling Peptides and Proteins*
Magnetic Resonance Spectroscopy
Peptides / chemistry
Phosphatidylglycerols* / chemistry

Substances

Intercellular Signaling Peptides and Proteins
Peptides
Phosphatidylglycerols