Surfactant protein B (SP-B), a component of lung surfactant (LS), plays an essential role in lowering the surface tension of alveoli, and in trafficking lipids to the air-fluid interface. Challenges in expressing native SP-B, have resulted in a number of synthetic peptide analogs being used to mimic its functionality for mechanistic studies and surfactant replacement therapies. Specifically, the terminal ends of SP-B, SP-Bc and SP-Bn, have retained certain functional properties of the protein and can be more easily studied. SP-Bc, is examined in comparison to its synthetic mimic, KL4, which is the main ingredient of a surfactant replacement known as Surfaxin .<br/><br/>In our studies, we utilize fluorescently labeled lipid probes, NBD-PE and Rhodamine-PE, to monitor membrane fusion events in DPPC:POPG and POPC:POPG liposomes using Fluorescence Resonance Energy Transfer (FRET). A decrease in FRET among the studied peptides will indicate increased rates of membrane fusion and may reveal a selective interaction with certain LS lipids. Current data displays a decrease in FRET within the DPPC:POPG SP-Bc system which supports previous NMR studies that showed the peptide selectively interacts with DPPC-rich liposomes and may indicate that SP-Bc facilitates membrane fusion events, which is a proposed mechanism of lipid trafficking at the air-fluid interface.

Using FRET to elucidate the lipid trafficking mechanism of SP-Bc and N terminal peptides in comparison with KL<sub>4</sub>

Macromolecular Chemistry: The Second Century

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ACS Spring 2020 National Meeting & Expo

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Using FRET to elucidate the lipid trafficking mechanism of SP-Bc and N terminal peptides in comparison with KL4

Using FRET to elucidate the lipid trafficking mechanism of SP-Bc and N terminal peptides in comparison with KL₄