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Sinapultide (also known as KL4 peptide) is a synthetic protein used to mimic human lung surfactant protein B. This protein has a weight of 2469.40. Sinapultide is a 21-residue peptide made up of lysine (K) and leucine (L) residues with the sequence KLLLLKLLLLKLLLLKLLLLK (KL4). In vitro assays demonstrated KL (4)-surfactant decreased neutrophil transmigration at the endothelial cell level. KL (4)-surfactant diminished inflammation and lung permeability when compared with controls in both mouse models of lung injury. >> Read More
KL4, a 21-residue peptide containing repeating KLLLL subunits, represents one of the early synthetic surfactant peptides designed to roughly reflect the overall ratio of cationic to hydrophobic amino acids found in native SP-B (22). Despite an early demonstration of SP-B-like activity and the fact that KL4 is currently under evaluation for FDA approval for clinical use as the peptide component of the synthetic exogenous surfactant Surfaxin (Lucinactant), surprisingly little is known about the specific effects of KL4 on phospholipid interfacial film behavior during compression/expansion and collapse.
KL4 Peptide Induces Reversible Collapse Structures on Multiple Length Scales in Model Lung Surfactant
KL4 ([lysine-(leucine)4]4-lysine) is a synthetic peptide based on SP-B structure and is the major constituent of Surfaxin®, a potential therapeutic agent for respiratory distress syndrome in premature infants. There is, however, no clear understanding about the possible lipid-KL4 interactions behind its function, which is an inevitable knowledge to design improved therapeutic agents. To examine the phase behavior, topography, and lipid specificity of KL4/lipid systems, we aimed to study different surfactant model systems containing KL4, neutral dipalmitoylphosphatidylcholine (DPPC) and/or negatively charged dipalmitoylphosphatidylglycerol (DPPG) in the presence of Ca2+ ions. Surface pressure-area isotherms, fluorescence microscopic images, scanning force microscopy as well as time-of-flight secondary ion mass spectrometry suggest that KL4 is not miscible with DPPC and therefore forms peptide aggregates in DPPC/KL4 mixtures; that KL4 specifically interacts with DPPG via electrostatic interactions and induces percolation of DPPG-rich phases; that existing DPPG-Ca2+ interactions are too strong to be overcome by KL4, the reason why the peptide remains excluded from condensed DPPG domains and passively colocalizes with DPPC in a demixed fluid phase; and that the presence of negatively charged lipid is necessary for the formation of bilayer protrusions. These results indicate that the capability of the peptide to induce the formation of a defined surface-confined reservoir depends on the lipid environment, especially on the presence of anionic lipids.
The Surfactant Peptide KL4 in Lipid Monolayers