Document Type
Article
Publication Date
7-1-2022
Publication Title
Biochimica et Biophysica Acta - Biomembranes
Volume
1864
Issue
7
Keywords
KL 4, Lung surfactant, Membranes
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).
DOI
10.1016/j.bbamem.2022.183893
ISSN
00052736
E-ISSN
18792642
Recommended Citation
Marquardt, Drew; van Oosten, Brad; Dziura, Maksymilian; Long, Joanna R.; and Harroun, Thad A.. (2022). The interaction and orientation of Peptide KL4 in model membranes. Biochimica et Biophysica Acta - Biomembranes, 1864 (7).
https://scholar.uwindsor.ca/chemistrybiochemistrypub/286
PubMed ID
35219719